data_9IT6
# 
_entry.id   9IT6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9IT6         pdb_00009it6 10.2210/pdb9it6/pdb 
WWPDB D_1300049611 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-01 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IT6 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9IS9 unspecified 
PDB . 9ISC unspecified 
PDB . 9ISE unspecified 
PDB . 9ISL unspecified 
PDB . 9ISR unspecified 
PDB . 9IT3 unspecified 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              suying@nhri.edu.tw 
_pdbx_contact_author.name_first         'Su Ying' 
_pdbx_contact_author.name_last          Wu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2816-6961 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lee, L.C.' 1 0000-0002-9210-0935 
'Wu, S.Y.'  2 0000-0003-2816-6961 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            67 
_citation.language                  ? 
_citation.page_first                21106 
_citation.page_last                 21125 
_citation.title                     
;Development of Potent and Selective Inhibitors of Methylenetetrahydrofolate Dehydrogenase 2 for Targeting Acute Myeloid Leukemia: SAR, Structural Insights, and Biological Characterization.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c01775 
_citation.pdbx_database_id_PubMed   39591507 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chang, H.H.'  1  ?                   
primary 'Lee, L.C.'    2  0000-0002-9210-0935 
primary 'Hsu, T.'      3  ?                   
primary 'Peng, Y.H.'   4  ?                   
primary 'Huang, C.H.'  5  ?                   
primary 'Yeh, T.K.'    6  ?                   
primary 'Lu, C.T.'     7  ?                   
primary 'Huang, Z.T.'  8  ?                   
primary 'Hsueh, C.C.'  9  ?                   
primary 'Kung, F.C.'   10 ?                   
primary 'Lin, L.M.'    11 ?                   
primary 'Huang, Y.C.'  12 ?                   
primary 'Wang, Y.H.'   13 ?                   
primary 'Li, L.H.'     14 ?                   
primary 'Tang, Y.C.'   15 ?                   
primary 'Chang, L.'    16 ?                   
primary 'Hsieh, C.C.'  17 ?                   
primary 'Jiaang, W.T.' 18 0000-0001-8781-3538 
primary 'Kuo, C.C.'    19 ?                   
primary 'Wu, S.Y.'     20 0000-0003-2816-6961 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial' 34597.020 2   
1.5.1.15,3.5.4.9 ? ? ? 
2 non-polymer syn 
;(2~{S})-2-[[4-[[2,4-bis(azanyl)-6-oxidanylidene-1~{H}-pyrimidin-5-yl]carbamoylamino]-3-chloranyl-phenyl]carbonylamino]-4-(1~{H}-1,2,3,4-tetrazol-5-yl)butanoic acid
;
491.849   2   ?                ? ? ? 
3 non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE 663.425   2   ?                ? ? ? 
4 non-polymer syn 'PHOSPHATE ION' 94.971    2   ?                ? ? ? 
5 water       nat water 18.015    188 ?                ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GSHMEAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPASISEE
ELLNLINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPT
LGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAV
IDVGINRVHDPVTAKPKLVGDVDFEGVRQKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKSKELGVATN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSHMEAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPASISEE
ELLNLINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPT
LGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAV
IDVGINRVHDPVTAKPKLVGDVDFEGVRQKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKSKELGVATN
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(2~{S})-2-[[4-[[2,4-bis(azanyl)-6-oxidanylidene-1~{H}-pyrimidin-5-yl]carbamoylamino]-3-chloranyl-phenyl]carbonylamino]-4-(1~{H}-1,2,3,4-tetrazol-5-yl)butanoic acid
;
A1L24 
3 NICOTINAMIDE-ADENINE-DINUCLEOTIDE NAD   
4 'PHOSPHATE ION' PO4   
5 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   HIS n 
1 4   MET n 
1 5   GLU n 
1 6   ALA n 
1 7   VAL n 
1 8   VAL n 
1 9   ILE n 
1 10  SER n 
1 11  GLY n 
1 12  ARG n 
1 13  LYS n 
1 14  LEU n 
1 15  ALA n 
1 16  GLN n 
1 17  GLN n 
1 18  ILE n 
1 19  LYS n 
1 20  GLN n 
1 21  GLU n 
1 22  VAL n 
1 23  ARG n 
1 24  GLN n 
1 25  GLU n 
1 26  VAL n 
1 27  GLU n 
1 28  GLU n 
1 29  TRP n 
1 30  VAL n 
1 31  ALA n 
1 32  SER n 
1 33  GLY n 
1 34  ASN n 
1 35  LYS n 
1 36  ARG n 
1 37  PRO n 
1 38  HIS n 
1 39  LEU n 
1 40  SER n 
1 41  VAL n 
1 42  ILE n 
1 43  LEU n 
1 44  VAL n 
1 45  GLY n 
1 46  GLU n 
1 47  ASN n 
1 48  PRO n 
1 49  ALA n 
1 50  SER n 
1 51  HIS n 
1 52  SER n 
1 53  TYR n 
1 54  VAL n 
1 55  LEU n 
1 56  ASN n 
1 57  LYS n 
1 58  THR n 
1 59  ARG n 
1 60  ALA n 
1 61  ALA n 
1 62  ALA n 
1 63  VAL n 
1 64  VAL n 
1 65  GLY n 
1 66  ILE n 
1 67  ASN n 
1 68  SER n 
1 69  GLU n 
1 70  THR n 
1 71  ILE n 
1 72  MET n 
1 73  LYS n 
1 74  PRO n 
1 75  ALA n 
1 76  SER n 
1 77  ILE n 
1 78  SER n 
1 79  GLU n 
1 80  GLU n 
1 81  GLU n 
1 82  LEU n 
1 83  LEU n 
1 84  ASN n 
1 85  LEU n 
1 86  ILE n 
1 87  ASN n 
1 88  LYS n 
1 89  LEU n 
1 90  ASN n 
1 91  ASN n 
1 92  ASP n 
1 93  ASP n 
1 94  ASN n 
1 95  VAL n 
1 96  ASP n 
1 97  GLY n 
1 98  LEU n 
1 99  LEU n 
1 100 VAL n 
1 101 GLN n 
1 102 LEU n 
1 103 PRO n 
1 104 LEU n 
1 105 PRO n 
1 106 GLU n 
1 107 HIS n 
1 108 ILE n 
1 109 ASP n 
1 110 GLU n 
1 111 ARG n 
1 112 ARG n 
1 113 ILE n 
1 114 CYS n 
1 115 ASN n 
1 116 ALA n 
1 117 VAL n 
1 118 SER n 
1 119 PRO n 
1 120 ASP n 
1 121 LYS n 
1 122 ASP n 
1 123 VAL n 
1 124 ASP n 
1 125 GLY n 
1 126 PHE n 
1 127 HIS n 
1 128 VAL n 
1 129 ILE n 
1 130 ASN n 
1 131 VAL n 
1 132 GLY n 
1 133 ARG n 
1 134 MET n 
1 135 CYS n 
1 136 LEU n 
1 137 ASP n 
1 138 GLN n 
1 139 TYR n 
1 140 SER n 
1 141 MET n 
1 142 LEU n 
1 143 PRO n 
1 144 ALA n 
1 145 THR n 
1 146 PRO n 
1 147 TRP n 
1 148 GLY n 
1 149 VAL n 
1 150 TRP n 
1 151 GLU n 
1 152 ILE n 
1 153 ILE n 
1 154 LYS n 
1 155 ARG n 
1 156 THR n 
1 157 GLY n 
1 158 ILE n 
1 159 PRO n 
1 160 THR n 
1 161 LEU n 
1 162 GLY n 
1 163 LYS n 
1 164 ASN n 
1 165 VAL n 
1 166 VAL n 
1 167 VAL n 
1 168 ALA n 
1 169 GLY n 
1 170 ARG n 
1 171 SER n 
1 172 LYS n 
1 173 ASN n 
1 174 VAL n 
1 175 GLY n 
1 176 MET n 
1 177 PRO n 
1 178 ILE n 
1 179 ALA n 
1 180 MET n 
1 181 LEU n 
1 182 LEU n 
1 183 HIS n 
1 184 THR n 
1 185 ASP n 
1 186 GLY n 
1 187 ALA n 
1 188 HIS n 
1 189 GLU n 
1 190 ARG n 
1 191 PRO n 
1 192 GLY n 
1 193 GLY n 
1 194 ASP n 
1 195 ALA n 
1 196 THR n 
1 197 VAL n 
1 198 THR n 
1 199 ILE n 
1 200 SER n 
1 201 HIS n 
1 202 ARG n 
1 203 TYR n 
1 204 THR n 
1 205 PRO n 
1 206 LYS n 
1 207 GLU n 
1 208 GLN n 
1 209 LEU n 
1 210 LYS n 
1 211 LYS n 
1 212 HIS n 
1 213 THR n 
1 214 ILE n 
1 215 LEU n 
1 216 ALA n 
1 217 ASP n 
1 218 ILE n 
1 219 VAL n 
1 220 ILE n 
1 221 SER n 
1 222 ALA n 
1 223 ALA n 
1 224 GLY n 
1 225 ILE n 
1 226 PRO n 
1 227 ASN n 
1 228 LEU n 
1 229 ILE n 
1 230 THR n 
1 231 ALA n 
1 232 ASP n 
1 233 MET n 
1 234 ILE n 
1 235 LYS n 
1 236 GLU n 
1 237 GLY n 
1 238 ALA n 
1 239 ALA n 
1 240 VAL n 
1 241 ILE n 
1 242 ASP n 
1 243 VAL n 
1 244 GLY n 
1 245 ILE n 
1 246 ASN n 
1 247 ARG n 
1 248 VAL n 
1 249 HIS n 
1 250 ASP n 
1 251 PRO n 
1 252 VAL n 
1 253 THR n 
1 254 ALA n 
1 255 LYS n 
1 256 PRO n 
1 257 LYS n 
1 258 LEU n 
1 259 VAL n 
1 260 GLY n 
1 261 ASP n 
1 262 VAL n 
1 263 ASP n 
1 264 PHE n 
1 265 GLU n 
1 266 GLY n 
1 267 VAL n 
1 268 ARG n 
1 269 GLN n 
1 270 LYS n 
1 271 ALA n 
1 272 GLY n 
1 273 TYR n 
1 274 ILE n 
1 275 THR n 
1 276 PRO n 
1 277 VAL n 
1 278 PRO n 
1 279 GLY n 
1 280 GLY n 
1 281 VAL n 
1 282 GLY n 
1 283 PRO n 
1 284 MET n 
1 285 THR n 
1 286 VAL n 
1 287 ALA n 
1 288 MET n 
1 289 LEU n 
1 290 MET n 
1 291 LYS n 
1 292 ASN n 
1 293 THR n 
1 294 ILE n 
1 295 ILE n 
1 296 ALA n 
1 297 ALA n 
1 298 LYS n 
1 299 LYS n 
1 300 VAL n 
1 301 LEU n 
1 302 ARG n 
1 303 LEU n 
1 304 GLU n 
1 305 GLU n 
1 306 ARG n 
1 307 GLU n 
1 308 VAL n 
1 309 LEU n 
1 310 LYS n 
1 311 SER n 
1 312 LYS n 
1 313 GLU n 
1 314 LEU n 
1 315 GLY n 
1 316 VAL n 
1 317 ALA n 
1 318 THR n 
1 319 ASN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   319 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'MTHFD2, NMDMC' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1L24 non-polymer         . 
;(2~{S})-2-[[4-[[2,4-bis(azanyl)-6-oxidanylidene-1~{H}-pyrimidin-5-yl]carbamoylamino]-3-chloranyl-phenyl]carbonylamino]-4-(1~{H}-1,2,3,4-tetrazol-5-yl)butanoic acid
;
? 'C17 H18 Cl N11 O5' 491.849 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'        133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'      121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER ? 'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'     149.211 
NAD   non-polymer         . NICOTINAMIDE-ADENINE-DINUCLEOTIDE ? 'C21 H27 N7 O14 P2' 663.425 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'       165.189 
PO4   non-polymer         . 'PHOSPHATE ION' ? 'O4 P -3'           94.971  
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   32  ?   ?   ?   A . n 
A 1 2   SER 2   33  ?   ?   ?   A . n 
A 1 3   HIS 3   34  ?   ?   ?   A . n 
A 1 4   MET 4   35  ?   ?   ?   A . n 
A 1 5   GLU 5   36  36  GLU GLU A . n 
A 1 6   ALA 6   37  37  ALA ALA A . n 
A 1 7   VAL 7   38  38  VAL VAL A . n 
A 1 8   VAL 8   39  39  VAL VAL A . n 
A 1 9   ILE 9   40  40  ILE ILE A . n 
A 1 10  SER 10  41  41  SER SER A . n 
A 1 11  GLY 11  42  42  GLY GLY A . n 
A 1 12  ARG 12  43  43  ARG ARG A . n 
A 1 13  LYS 13  44  44  LYS LYS A . n 
A 1 14  LEU 14  45  45  LEU LEU A . n 
A 1 15  ALA 15  46  46  ALA ALA A . n 
A 1 16  GLN 16  47  47  GLN GLN A . n 
A 1 17  GLN 17  48  48  GLN GLN A . n 
A 1 18  ILE 18  49  49  ILE ILE A . n 
A 1 19  LYS 19  50  50  LYS LYS A . n 
A 1 20  GLN 20  51  51  GLN GLN A . n 
A 1 21  GLU 21  52  52  GLU GLU A . n 
A 1 22  VAL 22  53  53  VAL VAL A . n 
A 1 23  ARG 23  54  54  ARG ARG A . n 
A 1 24  GLN 24  55  55  GLN GLN A . n 
A 1 25  GLU 25  56  56  GLU GLU A . n 
A 1 26  VAL 26  57  57  VAL VAL A . n 
A 1 27  GLU 27  58  58  GLU GLU A . n 
A 1 28  GLU 28  59  59  GLU GLU A . n 
A 1 29  TRP 29  60  60  TRP TRP A . n 
A 1 30  VAL 30  61  61  VAL VAL A . n 
A 1 31  ALA 31  62  62  ALA ALA A . n 
A 1 32  SER 32  63  63  SER SER A . n 
A 1 33  GLY 33  64  64  GLY GLY A . n 
A 1 34  ASN 34  65  65  ASN ASN A . n 
A 1 35  LYS 35  66  66  LYS LYS A . n 
A 1 36  ARG 36  67  67  ARG ARG A . n 
A 1 37  PRO 37  68  68  PRO PRO A . n 
A 1 38  HIS 38  69  69  HIS HIS A . n 
A 1 39  LEU 39  70  70  LEU LEU A . n 
A 1 40  SER 40  71  71  SER SER A . n 
A 1 41  VAL 41  72  72  VAL VAL A . n 
A 1 42  ILE 42  73  73  ILE ILE A . n 
A 1 43  LEU 43  74  74  LEU LEU A . n 
A 1 44  VAL 44  75  75  VAL VAL A . n 
A 1 45  GLY 45  76  76  GLY GLY A . n 
A 1 46  GLU 46  77  77  GLU GLU A . n 
A 1 47  ASN 47  78  78  ASN ASN A . n 
A 1 48  PRO 48  79  79  PRO PRO A . n 
A 1 49  ALA 49  80  80  ALA ALA A . n 
A 1 50  SER 50  81  81  SER SER A . n 
A 1 51  HIS 51  82  82  HIS HIS A . n 
A 1 52  SER 52  83  83  SER SER A . n 
A 1 53  TYR 53  84  84  TYR TYR A . n 
A 1 54  VAL 54  85  85  VAL VAL A . n 
A 1 55  LEU 55  86  86  LEU LEU A . n 
A 1 56  ASN 56  87  87  ASN ASN A . n 
A 1 57  LYS 57  88  88  LYS LYS A . n 
A 1 58  THR 58  89  89  THR THR A . n 
A 1 59  ARG 59  90  90  ARG ARG A . n 
A 1 60  ALA 60  91  91  ALA ALA A . n 
A 1 61  ALA 61  92  92  ALA ALA A . n 
A 1 62  ALA 62  93  93  ALA ALA A . n 
A 1 63  VAL 63  94  94  VAL VAL A . n 
A 1 64  VAL 64  95  95  VAL VAL A . n 
A 1 65  GLY 65  96  96  GLY GLY A . n 
A 1 66  ILE 66  97  97  ILE ILE A . n 
A 1 67  ASN 67  98  98  ASN ASN A . n 
A 1 68  SER 68  99  99  SER SER A . n 
A 1 69  GLU 69  100 100 GLU GLU A . n 
A 1 70  THR 70  101 101 THR THR A . n 
A 1 71  ILE 71  102 102 ILE ILE A . n 
A 1 72  MET 72  103 103 MET MET A . n 
A 1 73  LYS 73  104 104 LYS LYS A . n 
A 1 74  PRO 74  105 105 PRO PRO A . n 
A 1 75  ALA 75  106 106 ALA ALA A . n 
A 1 76  SER 76  107 107 SER SER A . n 
A 1 77  ILE 77  108 108 ILE ILE A . n 
A 1 78  SER 78  109 109 SER SER A . n 
A 1 79  GLU 79  110 110 GLU GLU A . n 
A 1 80  GLU 80  111 111 GLU GLU A . n 
A 1 81  GLU 81  112 112 GLU GLU A . n 
A 1 82  LEU 82  113 113 LEU LEU A . n 
A 1 83  LEU 83  114 114 LEU LEU A . n 
A 1 84  ASN 84  115 115 ASN ASN A . n 
A 1 85  LEU 85  116 116 LEU LEU A . n 
A 1 86  ILE 86  117 117 ILE ILE A . n 
A 1 87  ASN 87  118 118 ASN ASN A . n 
A 1 88  LYS 88  119 119 LYS LYS A . n 
A 1 89  LEU 89  120 120 LEU LEU A . n 
A 1 90  ASN 90  121 121 ASN ASN A . n 
A 1 91  ASN 91  122 122 ASN ASN A . n 
A 1 92  ASP 92  123 123 ASP ASP A . n 
A 1 93  ASP 93  124 124 ASP ASP A . n 
A 1 94  ASN 94  125 125 ASN ASN A . n 
A 1 95  VAL 95  126 126 VAL VAL A . n 
A 1 96  ASP 96  127 127 ASP ASP A . n 
A 1 97  GLY 97  128 128 GLY GLY A . n 
A 1 98  LEU 98  129 129 LEU LEU A . n 
A 1 99  LEU 99  130 130 LEU LEU A . n 
A 1 100 VAL 100 131 131 VAL VAL A . n 
A 1 101 GLN 101 132 132 GLN GLN A . n 
A 1 102 LEU 102 133 133 LEU LEU A . n 
A 1 103 PRO 103 134 134 PRO PRO A . n 
A 1 104 LEU 104 135 135 LEU LEU A . n 
A 1 105 PRO 105 136 136 PRO PRO A . n 
A 1 106 GLU 106 137 137 GLU GLU A . n 
A 1 107 HIS 107 138 138 HIS HIS A . n 
A 1 108 ILE 108 139 139 ILE ILE A . n 
A 1 109 ASP 109 140 140 ASP ASP A . n 
A 1 110 GLU 110 141 141 GLU GLU A . n 
A 1 111 ARG 111 142 142 ARG ARG A . n 
A 1 112 ARG 112 143 143 ARG ARG A . n 
A 1 113 ILE 113 144 144 ILE ILE A . n 
A 1 114 CYS 114 145 145 CYS CYS A . n 
A 1 115 ASN 115 146 146 ASN ASN A . n 
A 1 116 ALA 116 147 147 ALA ALA A . n 
A 1 117 VAL 117 148 148 VAL VAL A . n 
A 1 118 SER 118 149 149 SER SER A . n 
A 1 119 PRO 119 150 150 PRO PRO A . n 
A 1 120 ASP 120 151 151 ASP ASP A . n 
A 1 121 LYS 121 152 152 LYS LYS A . n 
A 1 122 ASP 122 153 153 ASP ASP A . n 
A 1 123 VAL 123 154 154 VAL VAL A . n 
A 1 124 ASP 124 155 155 ASP ASP A . n 
A 1 125 GLY 125 156 156 GLY GLY A . n 
A 1 126 PHE 126 157 157 PHE PHE A . n 
A 1 127 HIS 127 158 158 HIS HIS A . n 
A 1 128 VAL 128 159 159 VAL VAL A . n 
A 1 129 ILE 129 160 160 ILE ILE A . n 
A 1 130 ASN 130 161 161 ASN ASN A . n 
A 1 131 VAL 131 162 162 VAL VAL A . n 
A 1 132 GLY 132 163 163 GLY GLY A . n 
A 1 133 ARG 133 164 164 ARG ARG A . n 
A 1 134 MET 134 165 165 MET MET A . n 
A 1 135 CYS 135 166 166 CYS CYS A . n 
A 1 136 LEU 136 167 167 LEU LEU A . n 
A 1 137 ASP 137 168 168 ASP ASP A . n 
A 1 138 GLN 138 169 169 GLN GLN A . n 
A 1 139 TYR 139 170 170 TYR TYR A . n 
A 1 140 SER 140 171 171 SER SER A . n 
A 1 141 MET 141 172 172 MET MET A . n 
A 1 142 LEU 142 173 173 LEU LEU A . n 
A 1 143 PRO 143 174 174 PRO PRO A . n 
A 1 144 ALA 144 175 175 ALA ALA A . n 
A 1 145 THR 145 176 176 THR THR A . n 
A 1 146 PRO 146 177 177 PRO PRO A . n 
A 1 147 TRP 147 178 178 TRP TRP A . n 
A 1 148 GLY 148 179 179 GLY GLY A . n 
A 1 149 VAL 149 180 180 VAL VAL A . n 
A 1 150 TRP 150 181 181 TRP TRP A . n 
A 1 151 GLU 151 182 182 GLU GLU A . n 
A 1 152 ILE 152 183 183 ILE ILE A . n 
A 1 153 ILE 153 184 184 ILE ILE A . n 
A 1 154 LYS 154 185 185 LYS LYS A . n 
A 1 155 ARG 155 186 186 ARG ARG A . n 
A 1 156 THR 156 187 187 THR THR A . n 
A 1 157 GLY 157 188 188 GLY GLY A . n 
A 1 158 ILE 158 189 189 ILE ILE A . n 
A 1 159 PRO 159 190 190 PRO PRO A . n 
A 1 160 THR 160 191 191 THR THR A . n 
A 1 161 LEU 161 192 192 LEU LEU A . n 
A 1 162 GLY 162 193 193 GLY GLY A . n 
A 1 163 LYS 163 194 194 LYS LYS A . n 
A 1 164 ASN 164 195 195 ASN ASN A . n 
A 1 165 VAL 165 196 196 VAL VAL A . n 
A 1 166 VAL 166 197 197 VAL VAL A . n 
A 1 167 VAL 167 198 198 VAL VAL A . n 
A 1 168 ALA 168 199 199 ALA ALA A . n 
A 1 169 GLY 169 200 200 GLY GLY A . n 
A 1 170 ARG 170 201 201 ARG ARG A . n 
A 1 171 SER 171 202 202 SER SER A . n 
A 1 172 LYS 172 203 203 LYS LYS A . n 
A 1 173 ASN 173 204 204 ASN ASN A . n 
A 1 174 VAL 174 205 205 VAL VAL A . n 
A 1 175 GLY 175 206 206 GLY GLY A . n 
A 1 176 MET 176 207 207 MET MET A . n 
A 1 177 PRO 177 208 208 PRO PRO A . n 
A 1 178 ILE 178 209 209 ILE ILE A . n 
A 1 179 ALA 179 210 210 ALA ALA A . n 
A 1 180 MET 180 211 211 MET MET A . n 
A 1 181 LEU 181 212 212 LEU LEU A . n 
A 1 182 LEU 182 213 213 LEU LEU A . n 
A 1 183 HIS 183 214 214 HIS HIS A . n 
A 1 184 THR 184 215 215 THR THR A . n 
A 1 185 ASP 185 216 216 ASP ASP A . n 
A 1 186 GLY 186 217 217 GLY GLY A . n 
A 1 187 ALA 187 218 218 ALA ALA A . n 
A 1 188 HIS 188 219 219 HIS HIS A . n 
A 1 189 GLU 189 220 220 GLU GLU A . n 
A 1 190 ARG 190 221 221 ARG ARG A . n 
A 1 191 PRO 191 222 222 PRO PRO A . n 
A 1 192 GLY 192 223 223 GLY GLY A . n 
A 1 193 GLY 193 224 224 GLY GLY A . n 
A 1 194 ASP 194 225 225 ASP ASP A . n 
A 1 195 ALA 195 226 226 ALA ALA A . n 
A 1 196 THR 196 227 227 THR THR A . n 
A 1 197 VAL 197 228 228 VAL VAL A . n 
A 1 198 THR 198 229 229 THR THR A . n 
A 1 199 ILE 199 230 230 ILE ILE A . n 
A 1 200 SER 200 231 231 SER SER A . n 
A 1 201 HIS 201 232 232 HIS HIS A . n 
A 1 202 ARG 202 233 233 ARG ARG A . n 
A 1 203 TYR 203 234 234 TYR TYR A . n 
A 1 204 THR 204 235 235 THR THR A . n 
A 1 205 PRO 205 236 236 PRO PRO A . n 
A 1 206 LYS 206 237 237 LYS LYS A . n 
A 1 207 GLU 207 238 238 GLU GLU A . n 
A 1 208 GLN 208 239 239 GLN GLN A . n 
A 1 209 LEU 209 240 240 LEU LEU A . n 
A 1 210 LYS 210 241 241 LYS LYS A . n 
A 1 211 LYS 211 242 242 LYS LYS A . n 
A 1 212 HIS 212 243 243 HIS HIS A . n 
A 1 213 THR 213 244 244 THR THR A . n 
A 1 214 ILE 214 245 245 ILE ILE A . n 
A 1 215 LEU 215 246 246 LEU LEU A . n 
A 1 216 ALA 216 247 247 ALA ALA A . n 
A 1 217 ASP 217 248 248 ASP ASP A . n 
A 1 218 ILE 218 249 249 ILE ILE A . n 
A 1 219 VAL 219 250 250 VAL VAL A . n 
A 1 220 ILE 220 251 251 ILE ILE A . n 
A 1 221 SER 221 252 252 SER SER A . n 
A 1 222 ALA 222 253 253 ALA ALA A . n 
A 1 223 ALA 223 254 254 ALA ALA A . n 
A 1 224 GLY 224 255 255 GLY GLY A . n 
A 1 225 ILE 225 256 256 ILE ILE A . n 
A 1 226 PRO 226 257 257 PRO PRO A . n 
A 1 227 ASN 227 258 258 ASN ASN A . n 
A 1 228 LEU 228 259 259 LEU LEU A . n 
A 1 229 ILE 229 260 260 ILE ILE A . n 
A 1 230 THR 230 261 261 THR THR A . n 
A 1 231 ALA 231 262 262 ALA ALA A . n 
A 1 232 ASP 232 263 263 ASP ASP A . n 
A 1 233 MET 233 264 264 MET MET A . n 
A 1 234 ILE 234 265 265 ILE ILE A . n 
A 1 235 LYS 235 266 266 LYS LYS A . n 
A 1 236 GLU 236 267 267 GLU GLU A . n 
A 1 237 GLY 237 268 268 GLY GLY A . n 
A 1 238 ALA 238 269 269 ALA ALA A . n 
A 1 239 ALA 239 270 270 ALA ALA A . n 
A 1 240 VAL 240 271 271 VAL VAL A . n 
A 1 241 ILE 241 272 272 ILE ILE A . n 
A 1 242 ASP 242 273 273 ASP ASP A . n 
A 1 243 VAL 243 274 274 VAL VAL A . n 
A 1 244 GLY 244 275 275 GLY GLY A . n 
A 1 245 ILE 245 276 276 ILE ILE A . n 
A 1 246 ASN 246 277 277 ASN ASN A . n 
A 1 247 ARG 247 278 278 ARG ARG A . n 
A 1 248 VAL 248 279 279 VAL VAL A . n 
A 1 249 HIS 249 280 ?   ?   ?   A . n 
A 1 250 ASP 250 281 ?   ?   ?   A . n 
A 1 251 PRO 251 282 ?   ?   ?   A . n 
A 1 252 VAL 252 283 ?   ?   ?   A . n 
A 1 253 THR 253 284 ?   ?   ?   A . n 
A 1 254 ALA 254 285 ?   ?   ?   A . n 
A 1 255 LYS 255 286 ?   ?   ?   A . n 
A 1 256 PRO 256 287 ?   ?   ?   A . n 
A 1 257 LYS 257 288 288 LYS LYS A . n 
A 1 258 LEU 258 289 289 LEU LEU A . n 
A 1 259 VAL 259 290 290 VAL VAL A . n 
A 1 260 GLY 260 291 291 GLY GLY A . n 
A 1 261 ASP 261 292 292 ASP ASP A . n 
A 1 262 VAL 262 293 293 VAL VAL A . n 
A 1 263 ASP 263 294 294 ASP ASP A . n 
A 1 264 PHE 264 295 295 PHE PHE A . n 
A 1 265 GLU 265 296 296 GLU GLU A . n 
A 1 266 GLY 266 297 297 GLY GLY A . n 
A 1 267 VAL 267 298 298 VAL VAL A . n 
A 1 268 ARG 268 299 299 ARG ARG A . n 
A 1 269 GLN 269 300 300 GLN GLN A . n 
A 1 270 LYS 270 301 301 LYS LYS A . n 
A 1 271 ALA 271 302 302 ALA ALA A . n 
A 1 272 GLY 272 303 303 GLY GLY A . n 
A 1 273 TYR 273 304 304 TYR TYR A . n 
A 1 274 ILE 274 305 305 ILE ILE A . n 
A 1 275 THR 275 306 306 THR THR A . n 
A 1 276 PRO 276 307 307 PRO PRO A . n 
A 1 277 VAL 277 308 308 VAL VAL A . n 
A 1 278 PRO 278 309 309 PRO PRO A . n 
A 1 279 GLY 279 310 310 GLY GLY A . n 
A 1 280 GLY 280 311 311 GLY GLY A . n 
A 1 281 VAL 281 312 312 VAL VAL A . n 
A 1 282 GLY 282 313 313 GLY GLY A . n 
A 1 283 PRO 283 314 314 PRO PRO A . n 
A 1 284 MET 284 315 315 MET MET A . n 
A 1 285 THR 285 316 316 THR THR A . n 
A 1 286 VAL 286 317 317 VAL VAL A . n 
A 1 287 ALA 287 318 318 ALA ALA A . n 
A 1 288 MET 288 319 319 MET MET A . n 
A 1 289 LEU 289 320 320 LEU LEU A . n 
A 1 290 MET 290 321 321 MET MET A . n 
A 1 291 LYS 291 322 322 LYS LYS A . n 
A 1 292 ASN 292 323 323 ASN ASN A . n 
A 1 293 THR 293 324 324 THR THR A . n 
A 1 294 ILE 294 325 325 ILE ILE A . n 
A 1 295 ILE 295 326 326 ILE ILE A . n 
A 1 296 ALA 296 327 327 ALA ALA A . n 
A 1 297 ALA 297 328 328 ALA ALA A . n 
A 1 298 LYS 298 329 329 LYS LYS A . n 
A 1 299 LYS 299 330 330 LYS LYS A . n 
A 1 300 VAL 300 331 331 VAL VAL A . n 
A 1 301 LEU 301 332 332 LEU LEU A . n 
A 1 302 ARG 302 333 ?   ?   ?   A . n 
A 1 303 LEU 303 334 ?   ?   ?   A . n 
A 1 304 GLU 304 335 ?   ?   ?   A . n 
A 1 305 GLU 305 336 ?   ?   ?   A . n 
A 1 306 ARG 306 337 ?   ?   ?   A . n 
A 1 307 GLU 307 338 ?   ?   ?   A . n 
A 1 308 VAL 308 339 ?   ?   ?   A . n 
A 1 309 LEU 309 340 ?   ?   ?   A . n 
A 1 310 LYS 310 341 ?   ?   ?   A . n 
A 1 311 SER 311 342 ?   ?   ?   A . n 
A 1 312 LYS 312 343 ?   ?   ?   A . n 
A 1 313 GLU 313 344 ?   ?   ?   A . n 
A 1 314 LEU 314 345 ?   ?   ?   A . n 
A 1 315 GLY 315 346 ?   ?   ?   A . n 
A 1 316 VAL 316 347 ?   ?   ?   A . n 
A 1 317 ALA 317 348 ?   ?   ?   A . n 
A 1 318 THR 318 349 ?   ?   ?   A . n 
A 1 319 ASN 319 350 ?   ?   ?   A . n 
B 1 1   GLY 1   32  ?   ?   ?   B . n 
B 1 2   SER 2   33  ?   ?   ?   B . n 
B 1 3   HIS 3   34  ?   ?   ?   B . n 
B 1 4   MET 4   35  ?   ?   ?   B . n 
B 1 5   GLU 5   36  36  GLU GLU B . n 
B 1 6   ALA 6   37  37  ALA ALA B . n 
B 1 7   VAL 7   38  38  VAL VAL B . n 
B 1 8   VAL 8   39  39  VAL VAL B . n 
B 1 9   ILE 9   40  40  ILE ILE B . n 
B 1 10  SER 10  41  41  SER SER B . n 
B 1 11  GLY 11  42  42  GLY GLY B . n 
B 1 12  ARG 12  43  43  ARG ARG B . n 
B 1 13  LYS 13  44  44  LYS LYS B . n 
B 1 14  LEU 14  45  45  LEU LEU B . n 
B 1 15  ALA 15  46  46  ALA ALA B . n 
B 1 16  GLN 16  47  47  GLN GLN B . n 
B 1 17  GLN 17  48  48  GLN GLN B . n 
B 1 18  ILE 18  49  49  ILE ILE B . n 
B 1 19  LYS 19  50  50  LYS LYS B . n 
B 1 20  GLN 20  51  51  GLN GLN B . n 
B 1 21  GLU 21  52  52  GLU GLU B . n 
B 1 22  VAL 22  53  53  VAL VAL B . n 
B 1 23  ARG 23  54  54  ARG ARG B . n 
B 1 24  GLN 24  55  55  GLN GLN B . n 
B 1 25  GLU 25  56  56  GLU GLU B . n 
B 1 26  VAL 26  57  57  VAL VAL B . n 
B 1 27  GLU 27  58  58  GLU GLU B . n 
B 1 28  GLU 28  59  59  GLU GLU B . n 
B 1 29  TRP 29  60  60  TRP TRP B . n 
B 1 30  VAL 30  61  61  VAL VAL B . n 
B 1 31  ALA 31  62  62  ALA ALA B . n 
B 1 32  SER 32  63  63  SER SER B . n 
B 1 33  GLY 33  64  64  GLY GLY B . n 
B 1 34  ASN 34  65  65  ASN ASN B . n 
B 1 35  LYS 35  66  66  LYS LYS B . n 
B 1 36  ARG 36  67  67  ARG ARG B . n 
B 1 37  PRO 37  68  68  PRO PRO B . n 
B 1 38  HIS 38  69  69  HIS HIS B . n 
B 1 39  LEU 39  70  70  LEU LEU B . n 
B 1 40  SER 40  71  71  SER SER B . n 
B 1 41  VAL 41  72  72  VAL VAL B . n 
B 1 42  ILE 42  73  73  ILE ILE B . n 
B 1 43  LEU 43  74  74  LEU LEU B . n 
B 1 44  VAL 44  75  75  VAL VAL B . n 
B 1 45  GLY 45  76  76  GLY GLY B . n 
B 1 46  GLU 46  77  77  GLU GLU B . n 
B 1 47  ASN 47  78  78  ASN ASN B . n 
B 1 48  PRO 48  79  79  PRO PRO B . n 
B 1 49  ALA 49  80  80  ALA ALA B . n 
B 1 50  SER 50  81  81  SER SER B . n 
B 1 51  HIS 51  82  82  HIS HIS B . n 
B 1 52  SER 52  83  83  SER SER B . n 
B 1 53  TYR 53  84  84  TYR TYR B . n 
B 1 54  VAL 54  85  85  VAL VAL B . n 
B 1 55  LEU 55  86  86  LEU LEU B . n 
B 1 56  ASN 56  87  87  ASN ASN B . n 
B 1 57  LYS 57  88  88  LYS LYS B . n 
B 1 58  THR 58  89  89  THR THR B . n 
B 1 59  ARG 59  90  90  ARG ARG B . n 
B 1 60  ALA 60  91  91  ALA ALA B . n 
B 1 61  ALA 61  92  92  ALA ALA B . n 
B 1 62  ALA 62  93  93  ALA ALA B . n 
B 1 63  VAL 63  94  94  VAL VAL B . n 
B 1 64  VAL 64  95  95  VAL VAL B . n 
B 1 65  GLY 65  96  96  GLY GLY B . n 
B 1 66  ILE 66  97  97  ILE ILE B . n 
B 1 67  ASN 67  98  98  ASN ASN B . n 
B 1 68  SER 68  99  99  SER SER B . n 
B 1 69  GLU 69  100 100 GLU GLU B . n 
B 1 70  THR 70  101 101 THR THR B . n 
B 1 71  ILE 71  102 102 ILE ILE B . n 
B 1 72  MET 72  103 103 MET MET B . n 
B 1 73  LYS 73  104 104 LYS LYS B . n 
B 1 74  PRO 74  105 105 PRO PRO B . n 
B 1 75  ALA 75  106 106 ALA ALA B . n 
B 1 76  SER 76  107 107 SER SER B . n 
B 1 77  ILE 77  108 108 ILE ILE B . n 
B 1 78  SER 78  109 109 SER SER B . n 
B 1 79  GLU 79  110 110 GLU GLU B . n 
B 1 80  GLU 80  111 111 GLU GLU B . n 
B 1 81  GLU 81  112 112 GLU GLU B . n 
B 1 82  LEU 82  113 113 LEU LEU B . n 
B 1 83  LEU 83  114 114 LEU LEU B . n 
B 1 84  ASN 84  115 115 ASN ASN B . n 
B 1 85  LEU 85  116 116 LEU LEU B . n 
B 1 86  ILE 86  117 117 ILE ILE B . n 
B 1 87  ASN 87  118 118 ASN ASN B . n 
B 1 88  LYS 88  119 119 LYS LYS B . n 
B 1 89  LEU 89  120 120 LEU LEU B . n 
B 1 90  ASN 90  121 121 ASN ASN B . n 
B 1 91  ASN 91  122 122 ASN ASN B . n 
B 1 92  ASP 92  123 123 ASP ASP B . n 
B 1 93  ASP 93  124 124 ASP ASP B . n 
B 1 94  ASN 94  125 125 ASN ASN B . n 
B 1 95  VAL 95  126 126 VAL VAL B . n 
B 1 96  ASP 96  127 127 ASP ASP B . n 
B 1 97  GLY 97  128 128 GLY GLY B . n 
B 1 98  LEU 98  129 129 LEU LEU B . n 
B 1 99  LEU 99  130 130 LEU LEU B . n 
B 1 100 VAL 100 131 131 VAL VAL B . n 
B 1 101 GLN 101 132 132 GLN GLN B . n 
B 1 102 LEU 102 133 133 LEU LEU B . n 
B 1 103 PRO 103 134 134 PRO PRO B . n 
B 1 104 LEU 104 135 135 LEU LEU B . n 
B 1 105 PRO 105 136 136 PRO PRO B . n 
B 1 106 GLU 106 137 137 GLU GLU B . n 
B 1 107 HIS 107 138 138 HIS HIS B . n 
B 1 108 ILE 108 139 139 ILE ILE B . n 
B 1 109 ASP 109 140 140 ASP ASP B . n 
B 1 110 GLU 110 141 141 GLU GLU B . n 
B 1 111 ARG 111 142 142 ARG ARG B . n 
B 1 112 ARG 112 143 143 ARG ARG B . n 
B 1 113 ILE 113 144 144 ILE ILE B . n 
B 1 114 CYS 114 145 145 CYS CYS B . n 
B 1 115 ASN 115 146 146 ASN ASN B . n 
B 1 116 ALA 116 147 147 ALA ALA B . n 
B 1 117 VAL 117 148 148 VAL VAL B . n 
B 1 118 SER 118 149 149 SER SER B . n 
B 1 119 PRO 119 150 150 PRO PRO B . n 
B 1 120 ASP 120 151 151 ASP ASP B . n 
B 1 121 LYS 121 152 152 LYS LYS B . n 
B 1 122 ASP 122 153 153 ASP ASP B . n 
B 1 123 VAL 123 154 154 VAL VAL B . n 
B 1 124 ASP 124 155 155 ASP ASP B . n 
B 1 125 GLY 125 156 156 GLY GLY B . n 
B 1 126 PHE 126 157 157 PHE PHE B . n 
B 1 127 HIS 127 158 158 HIS HIS B . n 
B 1 128 VAL 128 159 159 VAL VAL B . n 
B 1 129 ILE 129 160 160 ILE ILE B . n 
B 1 130 ASN 130 161 161 ASN ASN B . n 
B 1 131 VAL 131 162 162 VAL VAL B . n 
B 1 132 GLY 132 163 163 GLY GLY B . n 
B 1 133 ARG 133 164 164 ARG ARG B . n 
B 1 134 MET 134 165 165 MET MET B . n 
B 1 135 CYS 135 166 166 CYS CYS B . n 
B 1 136 LEU 136 167 167 LEU LEU B . n 
B 1 137 ASP 137 168 168 ASP ASP B . n 
B 1 138 GLN 138 169 169 GLN GLN B . n 
B 1 139 TYR 139 170 170 TYR TYR B . n 
B 1 140 SER 140 171 171 SER SER B . n 
B 1 141 MET 141 172 172 MET MET B . n 
B 1 142 LEU 142 173 173 LEU LEU B . n 
B 1 143 PRO 143 174 174 PRO PRO B . n 
B 1 144 ALA 144 175 175 ALA ALA B . n 
B 1 145 THR 145 176 176 THR THR B . n 
B 1 146 PRO 146 177 177 PRO PRO B . n 
B 1 147 TRP 147 178 178 TRP TRP B . n 
B 1 148 GLY 148 179 179 GLY GLY B . n 
B 1 149 VAL 149 180 180 VAL VAL B . n 
B 1 150 TRP 150 181 181 TRP TRP B . n 
B 1 151 GLU 151 182 182 GLU GLU B . n 
B 1 152 ILE 152 183 183 ILE ILE B . n 
B 1 153 ILE 153 184 184 ILE ILE B . n 
B 1 154 LYS 154 185 185 LYS LYS B . n 
B 1 155 ARG 155 186 186 ARG ARG B . n 
B 1 156 THR 156 187 187 THR THR B . n 
B 1 157 GLY 157 188 188 GLY GLY B . n 
B 1 158 ILE 158 189 189 ILE ILE B . n 
B 1 159 PRO 159 190 190 PRO PRO B . n 
B 1 160 THR 160 191 191 THR THR B . n 
B 1 161 LEU 161 192 192 LEU LEU B . n 
B 1 162 GLY 162 193 193 GLY GLY B . n 
B 1 163 LYS 163 194 194 LYS LYS B . n 
B 1 164 ASN 164 195 195 ASN ASN B . n 
B 1 165 VAL 165 196 196 VAL VAL B . n 
B 1 166 VAL 166 197 197 VAL VAL B . n 
B 1 167 VAL 167 198 198 VAL VAL B . n 
B 1 168 ALA 168 199 199 ALA ALA B . n 
B 1 169 GLY 169 200 200 GLY GLY B . n 
B 1 170 ARG 170 201 201 ARG ARG B . n 
B 1 171 SER 171 202 202 SER SER B . n 
B 1 172 LYS 172 203 203 LYS LYS B . n 
B 1 173 ASN 173 204 204 ASN ASN B . n 
B 1 174 VAL 174 205 205 VAL VAL B . n 
B 1 175 GLY 175 206 206 GLY GLY B . n 
B 1 176 MET 176 207 207 MET MET B . n 
B 1 177 PRO 177 208 208 PRO PRO B . n 
B 1 178 ILE 178 209 209 ILE ILE B . n 
B 1 179 ALA 179 210 210 ALA ALA B . n 
B 1 180 MET 180 211 211 MET MET B . n 
B 1 181 LEU 181 212 212 LEU LEU B . n 
B 1 182 LEU 182 213 213 LEU LEU B . n 
B 1 183 HIS 183 214 214 HIS HIS B . n 
B 1 184 THR 184 215 215 THR THR B . n 
B 1 185 ASP 185 216 216 ASP ASP B . n 
B 1 186 GLY 186 217 217 GLY GLY B . n 
B 1 187 ALA 187 218 218 ALA ALA B . n 
B 1 188 HIS 188 219 219 HIS HIS B . n 
B 1 189 GLU 189 220 220 GLU GLU B . n 
B 1 190 ARG 190 221 221 ARG ARG B . n 
B 1 191 PRO 191 222 222 PRO PRO B . n 
B 1 192 GLY 192 223 223 GLY GLY B . n 
B 1 193 GLY 193 224 224 GLY GLY B . n 
B 1 194 ASP 194 225 225 ASP ASP B . n 
B 1 195 ALA 195 226 226 ALA ALA B . n 
B 1 196 THR 196 227 227 THR THR B . n 
B 1 197 VAL 197 228 228 VAL VAL B . n 
B 1 198 THR 198 229 229 THR THR B . n 
B 1 199 ILE 199 230 230 ILE ILE B . n 
B 1 200 SER 200 231 231 SER SER B . n 
B 1 201 HIS 201 232 232 HIS HIS B . n 
B 1 202 ARG 202 233 233 ARG ARG B . n 
B 1 203 TYR 203 234 234 TYR TYR B . n 
B 1 204 THR 204 235 235 THR THR B . n 
B 1 205 PRO 205 236 236 PRO PRO B . n 
B 1 206 LYS 206 237 237 LYS LYS B . n 
B 1 207 GLU 207 238 238 GLU GLU B . n 
B 1 208 GLN 208 239 239 GLN GLN B . n 
B 1 209 LEU 209 240 240 LEU LEU B . n 
B 1 210 LYS 210 241 241 LYS LYS B . n 
B 1 211 LYS 211 242 242 LYS LYS B . n 
B 1 212 HIS 212 243 243 HIS HIS B . n 
B 1 213 THR 213 244 244 THR THR B . n 
B 1 214 ILE 214 245 245 ILE ILE B . n 
B 1 215 LEU 215 246 246 LEU LEU B . n 
B 1 216 ALA 216 247 247 ALA ALA B . n 
B 1 217 ASP 217 248 248 ASP ASP B . n 
B 1 218 ILE 218 249 249 ILE ILE B . n 
B 1 219 VAL 219 250 250 VAL VAL B . n 
B 1 220 ILE 220 251 251 ILE ILE B . n 
B 1 221 SER 221 252 252 SER SER B . n 
B 1 222 ALA 222 253 253 ALA ALA B . n 
B 1 223 ALA 223 254 254 ALA ALA B . n 
B 1 224 GLY 224 255 255 GLY GLY B . n 
B 1 225 ILE 225 256 256 ILE ILE B . n 
B 1 226 PRO 226 257 257 PRO PRO B . n 
B 1 227 ASN 227 258 258 ASN ASN B . n 
B 1 228 LEU 228 259 259 LEU LEU B . n 
B 1 229 ILE 229 260 260 ILE ILE B . n 
B 1 230 THR 230 261 261 THR THR B . n 
B 1 231 ALA 231 262 262 ALA ALA B . n 
B 1 232 ASP 232 263 263 ASP ASP B . n 
B 1 233 MET 233 264 264 MET MET B . n 
B 1 234 ILE 234 265 265 ILE ILE B . n 
B 1 235 LYS 235 266 266 LYS LYS B . n 
B 1 236 GLU 236 267 267 GLU GLU B . n 
B 1 237 GLY 237 268 268 GLY GLY B . n 
B 1 238 ALA 238 269 269 ALA ALA B . n 
B 1 239 ALA 239 270 270 ALA ALA B . n 
B 1 240 VAL 240 271 271 VAL VAL B . n 
B 1 241 ILE 241 272 272 ILE ILE B . n 
B 1 242 ASP 242 273 273 ASP ASP B . n 
B 1 243 VAL 243 274 274 VAL VAL B . n 
B 1 244 GLY 244 275 275 GLY GLY B . n 
B 1 245 ILE 245 276 276 ILE ILE B . n 
B 1 246 ASN 246 277 277 ASN ASN B . n 
B 1 247 ARG 247 278 278 ARG ARG B . n 
B 1 248 VAL 248 279 279 VAL VAL B . n 
B 1 249 HIS 249 280 280 HIS HIS B . n 
B 1 250 ASP 250 281 ?   ?   ?   B . n 
B 1 251 PRO 251 282 ?   ?   ?   B . n 
B 1 252 VAL 252 283 ?   ?   ?   B . n 
B 1 253 THR 253 284 ?   ?   ?   B . n 
B 1 254 ALA 254 285 ?   ?   ?   B . n 
B 1 255 LYS 255 286 ?   ?   ?   B . n 
B 1 256 PRO 256 287 ?   ?   ?   B . n 
B 1 257 LYS 257 288 288 LYS LYS B . n 
B 1 258 LEU 258 289 289 LEU LEU B . n 
B 1 259 VAL 259 290 290 VAL VAL B . n 
B 1 260 GLY 260 291 291 GLY GLY B . n 
B 1 261 ASP 261 292 292 ASP ASP B . n 
B 1 262 VAL 262 293 293 VAL VAL B . n 
B 1 263 ASP 263 294 294 ASP ASP B . n 
B 1 264 PHE 264 295 295 PHE PHE B . n 
B 1 265 GLU 265 296 296 GLU GLU B . n 
B 1 266 GLY 266 297 297 GLY GLY B . n 
B 1 267 VAL 267 298 298 VAL VAL B . n 
B 1 268 ARG 268 299 299 ARG ARG B . n 
B 1 269 GLN 269 300 300 GLN GLN B . n 
B 1 270 LYS 270 301 301 LYS LYS B . n 
B 1 271 ALA 271 302 302 ALA ALA B . n 
B 1 272 GLY 272 303 303 GLY GLY B . n 
B 1 273 TYR 273 304 304 TYR TYR B . n 
B 1 274 ILE 274 305 305 ILE ILE B . n 
B 1 275 THR 275 306 306 THR THR B . n 
B 1 276 PRO 276 307 307 PRO PRO B . n 
B 1 277 VAL 277 308 308 VAL VAL B . n 
B 1 278 PRO 278 309 309 PRO PRO B . n 
B 1 279 GLY 279 310 310 GLY GLY B . n 
B 1 280 GLY 280 311 311 GLY GLY B . n 
B 1 281 VAL 281 312 312 VAL VAL B . n 
B 1 282 GLY 282 313 313 GLY GLY B . n 
B 1 283 PRO 283 314 314 PRO PRO B . n 
B 1 284 MET 284 315 315 MET MET B . n 
B 1 285 THR 285 316 316 THR THR B . n 
B 1 286 VAL 286 317 317 VAL VAL B . n 
B 1 287 ALA 287 318 318 ALA ALA B . n 
B 1 288 MET 288 319 319 MET MET B . n 
B 1 289 LEU 289 320 320 LEU LEU B . n 
B 1 290 MET 290 321 321 MET MET B . n 
B 1 291 LYS 291 322 322 LYS LYS B . n 
B 1 292 ASN 292 323 323 ASN ASN B . n 
B 1 293 THR 293 324 324 THR THR B . n 
B 1 294 ILE 294 325 325 ILE ILE B . n 
B 1 295 ILE 295 326 326 ILE ILE B . n 
B 1 296 ALA 296 327 327 ALA ALA B . n 
B 1 297 ALA 297 328 328 ALA ALA B . n 
B 1 298 LYS 298 329 329 LYS LYS B . n 
B 1 299 LYS 299 330 330 LYS LYS B . n 
B 1 300 VAL 300 331 331 VAL VAL B . n 
B 1 301 LEU 301 332 332 LEU LEU B . n 
B 1 302 ARG 302 333 ?   ?   ?   B . n 
B 1 303 LEU 303 334 ?   ?   ?   B . n 
B 1 304 GLU 304 335 ?   ?   ?   B . n 
B 1 305 GLU 305 336 ?   ?   ?   B . n 
B 1 306 ARG 306 337 ?   ?   ?   B . n 
B 1 307 GLU 307 338 ?   ?   ?   B . n 
B 1 308 VAL 308 339 ?   ?   ?   B . n 
B 1 309 LEU 309 340 ?   ?   ?   B . n 
B 1 310 LYS 310 341 ?   ?   ?   B . n 
B 1 311 SER 311 342 ?   ?   ?   B . n 
B 1 312 LYS 312 343 ?   ?   ?   B . n 
B 1 313 GLU 313 344 ?   ?   ?   B . n 
B 1 314 LEU 314 345 ?   ?   ?   B . n 
B 1 315 GLY 315 346 ?   ?   ?   B . n 
B 1 316 VAL 316 347 ?   ?   ?   B . n 
B 1 317 ALA 317 348 ?   ?   ?   B . n 
B 1 318 THR 318 349 ?   ?   ?   B . n 
B 1 319 ASN 319 350 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1L24 1   401 401 A1L24 LIG A . 
D 3 NAD   1   402 501 NAD   NAD A . 
E 4 PO4   1   403 1   PO4   PO4 A . 
F 4 PO4   1   404 2   PO4   PO4 A . 
G 2 A1L24 1   401 401 A1L24 LIG B . 
H 3 NAD   1   402 501 NAD   NAD B . 
I 5 HOH   1   501 106 HOH   HOH A . 
I 5 HOH   2   502 12  HOH   HOH A . 
I 5 HOH   3   503 81  HOH   HOH A . 
I 5 HOH   4   504 130 HOH   HOH A . 
I 5 HOH   5   505 48  HOH   HOH A . 
I 5 HOH   6   506 42  HOH   HOH A . 
I 5 HOH   7   507 67  HOH   HOH A . 
I 5 HOH   8   508 165 HOH   HOH A . 
I 5 HOH   9   509 77  HOH   HOH A . 
I 5 HOH   10  510 63  HOH   HOH A . 
I 5 HOH   11  511 65  HOH   HOH A . 
I 5 HOH   12  512 71  HOH   HOH A . 
I 5 HOH   13  513 147 HOH   HOH A . 
I 5 HOH   14  514 133 HOH   HOH A . 
I 5 HOH   15  515 45  HOH   HOH A . 
I 5 HOH   16  516 168 HOH   HOH A . 
I 5 HOH   17  517 39  HOH   HOH A . 
I 5 HOH   18  518 36  HOH   HOH A . 
I 5 HOH   19  519 121 HOH   HOH A . 
I 5 HOH   20  520 2   HOH   HOH A . 
I 5 HOH   21  521 5   HOH   HOH A . 
I 5 HOH   22  522 181 HOH   HOH A . 
I 5 HOH   23  523 66  HOH   HOH A . 
I 5 HOH   24  524 31  HOH   HOH A . 
I 5 HOH   25  525 78  HOH   HOH A . 
I 5 HOH   26  526 10  HOH   HOH A . 
I 5 HOH   27  527 21  HOH   HOH A . 
I 5 HOH   28  528 175 HOH   HOH A . 
I 5 HOH   29  529 140 HOH   HOH A . 
I 5 HOH   30  530 160 HOH   HOH A . 
I 5 HOH   31  531 101 HOH   HOH A . 
I 5 HOH   32  532 145 HOH   HOH A . 
I 5 HOH   33  533 158 HOH   HOH A . 
I 5 HOH   34  534 185 HOH   HOH A . 
I 5 HOH   35  535 52  HOH   HOH A . 
I 5 HOH   36  536 23  HOH   HOH A . 
I 5 HOH   37  537 68  HOH   HOH A . 
I 5 HOH   38  538 144 HOH   HOH A . 
I 5 HOH   39  539 14  HOH   HOH A . 
I 5 HOH   40  540 108 HOH   HOH A . 
I 5 HOH   41  541 54  HOH   HOH A . 
I 5 HOH   42  542 33  HOH   HOH A . 
I 5 HOH   43  543 18  HOH   HOH A . 
I 5 HOH   44  544 72  HOH   HOH A . 
I 5 HOH   45  545 11  HOH   HOH A . 
I 5 HOH   46  546 122 HOH   HOH A . 
I 5 HOH   47  547 58  HOH   HOH A . 
I 5 HOH   48  548 76  HOH   HOH A . 
I 5 HOH   49  549 3   HOH   HOH A . 
I 5 HOH   50  550 29  HOH   HOH A . 
I 5 HOH   51  551 154 HOH   HOH A . 
I 5 HOH   52  552 15  HOH   HOH A . 
I 5 HOH   53  553 60  HOH   HOH A . 
I 5 HOH   54  554 40  HOH   HOH A . 
I 5 HOH   55  555 171 HOH   HOH A . 
I 5 HOH   56  556 178 HOH   HOH A . 
I 5 HOH   57  557 24  HOH   HOH A . 
I 5 HOH   58  558 162 HOH   HOH A . 
I 5 HOH   59  559 110 HOH   HOH A . 
I 5 HOH   60  560 28  HOH   HOH A . 
I 5 HOH   61  561 109 HOH   HOH A . 
I 5 HOH   62  562 37  HOH   HOH A . 
I 5 HOH   63  563 91  HOH   HOH A . 
I 5 HOH   64  564 75  HOH   HOH A . 
I 5 HOH   65  565 142 HOH   HOH A . 
I 5 HOH   66  566 9   HOH   HOH A . 
I 5 HOH   67  567 150 HOH   HOH A . 
I 5 HOH   68  568 180 HOH   HOH A . 
I 5 HOH   69  569 141 HOH   HOH A . 
I 5 HOH   70  570 7   HOH   HOH A . 
I 5 HOH   71  571 125 HOH   HOH A . 
I 5 HOH   72  572 148 HOH   HOH A . 
I 5 HOH   73  573 88  HOH   HOH A . 
I 5 HOH   74  574 49  HOH   HOH A . 
I 5 HOH   75  575 124 HOH   HOH A . 
I 5 HOH   76  576 41  HOH   HOH A . 
I 5 HOH   77  577 83  HOH   HOH A . 
I 5 HOH   78  578 20  HOH   HOH A . 
I 5 HOH   79  579 89  HOH   HOH A . 
I 5 HOH   80  580 90  HOH   HOH A . 
I 5 HOH   81  581 47  HOH   HOH A . 
I 5 HOH   82  582 79  HOH   HOH A . 
I 5 HOH   83  583 143 HOH   HOH A . 
I 5 HOH   84  584 184 HOH   HOH A . 
I 5 HOH   85  585 132 HOH   HOH A . 
I 5 HOH   86  586 98  HOH   HOH A . 
I 5 HOH   87  587 96  HOH   HOH A . 
I 5 HOH   88  588 183 HOH   HOH A . 
I 5 HOH   89  589 187 HOH   HOH A . 
I 5 HOH   90  590 74  HOH   HOH A . 
I 5 HOH   91  591 93  HOH   HOH A . 
I 5 HOH   92  592 126 HOH   HOH A . 
I 5 HOH   93  593 80  HOH   HOH A . 
I 5 HOH   94  594 163 HOH   HOH A . 
I 5 HOH   95  595 159 HOH   HOH A . 
I 5 HOH   96  596 151 HOH   HOH A . 
I 5 HOH   97  597 174 HOH   HOH A . 
I 5 HOH   98  598 164 HOH   HOH A . 
I 5 HOH   99  599 44  HOH   HOH A . 
I 5 HOH   100 600 59  HOH   HOH A . 
I 5 HOH   101 601 64  HOH   HOH A . 
I 5 HOH   102 602 114 HOH   HOH A . 
I 5 HOH   103 603 138 HOH   HOH A . 
J 5 HOH   1   501 19  HOH   HOH B . 
J 5 HOH   2   502 111 HOH   HOH B . 
J 5 HOH   3   503 82  HOH   HOH B . 
J 5 HOH   4   504 97  HOH   HOH B . 
J 5 HOH   5   505 55  HOH   HOH B . 
J 5 HOH   6   506 57  HOH   HOH B . 
J 5 HOH   7   507 120 HOH   HOH B . 
J 5 HOH   8   508 92  HOH   HOH B . 
J 5 HOH   9   509 26  HOH   HOH B . 
J 5 HOH   10  510 56  HOH   HOH B . 
J 5 HOH   11  511 30  HOH   HOH B . 
J 5 HOH   12  512 179 HOH   HOH B . 
J 5 HOH   13  513 135 HOH   HOH B . 
J 5 HOH   14  514 123 HOH   HOH B . 
J 5 HOH   15  515 4   HOH   HOH B . 
J 5 HOH   16  516 84  HOH   HOH B . 
J 5 HOH   17  517 85  HOH   HOH B . 
J 5 HOH   18  518 32  HOH   HOH B . 
J 5 HOH   19  519 153 HOH   HOH B . 
J 5 HOH   20  520 61  HOH   HOH B . 
J 5 HOH   21  521 177 HOH   HOH B . 
J 5 HOH   22  522 53  HOH   HOH B . 
J 5 HOH   23  523 112 HOH   HOH B . 
J 5 HOH   24  524 99  HOH   HOH B . 
J 5 HOH   25  525 94  HOH   HOH B . 
J 5 HOH   26  526 46  HOH   HOH B . 
J 5 HOH   27  527 22  HOH   HOH B . 
J 5 HOH   28  528 100 HOH   HOH B . 
J 5 HOH   29  529 166 HOH   HOH B . 
J 5 HOH   30  530 127 HOH   HOH B . 
J 5 HOH   31  531 50  HOH   HOH B . 
J 5 HOH   32  532 117 HOH   HOH B . 
J 5 HOH   33  533 134 HOH   HOH B . 
J 5 HOH   34  534 43  HOH   HOH B . 
J 5 HOH   35  535 17  HOH   HOH B . 
J 5 HOH   36  536 8   HOH   HOH B . 
J 5 HOH   37  537 169 HOH   HOH B . 
J 5 HOH   38  538 87  HOH   HOH B . 
J 5 HOH   39  539 6   HOH   HOH B . 
J 5 HOH   40  540 73  HOH   HOH B . 
J 5 HOH   41  541 157 HOH   HOH B . 
J 5 HOH   42  542 156 HOH   HOH B . 
J 5 HOH   43  543 137 HOH   HOH B . 
J 5 HOH   44  544 103 HOH   HOH B . 
J 5 HOH   45  545 136 HOH   HOH B . 
J 5 HOH   46  546 95  HOH   HOH B . 
J 5 HOH   47  547 62  HOH   HOH B . 
J 5 HOH   48  548 38  HOH   HOH B . 
J 5 HOH   49  549 152 HOH   HOH B . 
J 5 HOH   50  550 1   HOH   HOH B . 
J 5 HOH   51  551 34  HOH   HOH B . 
J 5 HOH   52  552 51  HOH   HOH B . 
J 5 HOH   53  553 129 HOH   HOH B . 
J 5 HOH   54  554 102 HOH   HOH B . 
J 5 HOH   55  555 149 HOH   HOH B . 
J 5 HOH   56  556 113 HOH   HOH B . 
J 5 HOH   57  557 25  HOH   HOH B . 
J 5 HOH   58  558 104 HOH   HOH B . 
J 5 HOH   59  559 118 HOH   HOH B . 
J 5 HOH   60  560 167 HOH   HOH B . 
J 5 HOH   61  561 13  HOH   HOH B . 
J 5 HOH   62  562 186 HOH   HOH B . 
J 5 HOH   63  563 119 HOH   HOH B . 
J 5 HOH   64  564 173 HOH   HOH B . 
J 5 HOH   65  565 128 HOH   HOH B . 
J 5 HOH   66  566 86  HOH   HOH B . 
J 5 HOH   67  567 176 HOH   HOH B . 
J 5 HOH   68  568 70  HOH   HOH B . 
J 5 HOH   69  569 16  HOH   HOH B . 
J 5 HOH   70  570 35  HOH   HOH B . 
J 5 HOH   71  571 172 HOH   HOH B . 
J 5 HOH   72  572 69  HOH   HOH B . 
J 5 HOH   73  573 139 HOH   HOH B . 
J 5 HOH   74  574 131 HOH   HOH B . 
J 5 HOH   75  575 182 HOH   HOH B . 
J 5 HOH   76  576 146 HOH   HOH B . 
J 5 HOH   77  577 155 HOH   HOH B . 
J 5 HOH   78  578 27  HOH   HOH B . 
J 5 HOH   79  579 161 HOH   HOH B . 
J 5 HOH   80  580 107 HOH   HOH B . 
J 5 HOH   81  581 188 HOH   HOH B . 
J 5 HOH   82  582 115 HOH   HOH B . 
J 5 HOH   83  583 105 HOH   HOH B . 
J 5 HOH   84  584 170 HOH   HOH B . 
J 5 HOH   85  585 116 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A MET 103 ? CG  ? A MET 72  CG  
2  1 Y 1 A MET 103 ? SD  ? A MET 72  SD  
3  1 Y 1 A MET 103 ? CE  ? A MET 72  CE  
4  1 Y 1 A ARG 278 ? CG  ? A ARG 247 CG  
5  1 Y 1 A ARG 278 ? CD  ? A ARG 247 CD  
6  1 Y 1 A ARG 278 ? NE  ? A ARG 247 NE  
7  1 Y 1 A ARG 278 ? CZ  ? A ARG 247 CZ  
8  1 Y 1 A ARG 278 ? NH1 ? A ARG 247 NH1 
9  1 Y 1 A ARG 278 ? NH2 ? A ARG 247 NH2 
10 1 Y 1 A VAL 279 ? CG1 ? A VAL 248 CG1 
11 1 Y 1 A VAL 279 ? CG2 ? A VAL 248 CG2 
12 1 Y 1 B GLU 137 ? CG  ? B GLU 106 CG  
13 1 Y 1 B GLU 137 ? CD  ? B GLU 106 CD  
14 1 Y 1 B GLU 137 ? OE1 ? B GLU 106 OE1 
15 1 Y 1 B GLU 137 ? OE2 ? B GLU 106 OE2 
16 1 Y 1 B ARG 278 ? CG  ? B ARG 247 CG  
17 1 Y 1 B ARG 278 ? CD  ? B ARG 247 CD  
18 1 Y 1 B ARG 278 ? NE  ? B ARG 247 NE  
19 1 Y 1 B ARG 278 ? CZ  ? B ARG 247 CZ  
20 1 Y 1 B ARG 278 ? NH1 ? B ARG 247 NH1 
21 1 Y 1 B ARG 278 ? NH2 ? B ARG 247 NH2 
22 1 Y 1 B VAL 279 ? CG1 ? B VAL 248 CG1 
23 1 Y 1 B VAL 279 ? CG2 ? B VAL 248 CG2 
24 1 Y 1 B HIS 280 ? CG  ? B HIS 249 CG  
25 1 Y 1 B HIS 280 ? ND1 ? B HIS 249 ND1 
26 1 Y 1 B HIS 280 ? CD2 ? B HIS 249 CD2 
27 1 Y 1 B HIS 280 ? CE1 ? B HIS 249 CE1 
28 1 Y 1 B HIS 280 ? NE2 ? B HIS 249 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? '(1.21.1_5286: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000  ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP    ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IT6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     114.849 
_cell.length_a_esd                 ? 
_cell.length_b                     114.849 
_cell.length_b_esd                 ? 
_cell.length_c                     113.413 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9IT6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                170 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 65' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IT6 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.12 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          60.58 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'isopropanol, Bis-Tris pH 7.1, PEG 400' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-07-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SPRING-8 BEAMLINE BL44XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL44XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9IT6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.04 
_reflns.d_resolution_low                               30.00 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     53789 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.062 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.04 2.11  ? ? ? ? ? ? 5369 ? ? ? ? ? ? ? ? ? ? ? 4.2 1.033 ? ? 0.541 0.252 ? 1  1 0.818 0.948 ? 99.8  ? 0.473 ? ? ? ? ? ? ? ? ? 
2.11 2.20  ? ? ? ? ? ? 5380 ? ? ? ? ? ? ? ? ? ? ? 4.3 1.000 ? ? 0.377 0.175 ? 2  1 0.902 0.974 ? 100.0 ? 0.330 ? ? ? ? ? ? ? ? ? 
2.20 2.30  ? ? ? ? ? ? 5390 ? ? ? ? ? ? ? ? ? ? ? 4.2 1.065 ? ? 0.293 0.137 ? 3  1 0.925 0.980 ? 99.6  ? 0.255 ? ? ? ? ? ? ? ? ? 
2.30 2.42  ? ? ? ? ? ? 5418 ? ? ? ? ? ? ? ? ? ? ? 4.3 1.007 ? ? 0.212 0.097 ? 4  1 0.966 0.991 ? 100.0 ? 0.186 ? ? ? ? ? ? ? ? ? 
2.42 2.57  ? ? ? ? ? ? 5394 ? ? ? ? ? ? ? ? ? ? ? 4.2 1.068 ? ? 0.156 0.070 ? 5  1 0.982 0.996 ? 100.0 ? 0.137 ? ? ? ? ? ? ? ? ? 
2.57 2.77  ? ? ? ? ? ? 5397 ? ? ? ? ? ? ? ? ? ? ? 4.2 1.020 ? ? 0.119 0.053 ? 6  1 0.989 0.997 ? 99.9  ? 0.105 ? ? ? ? ? ? ? ? ? 
2.77 3.05  ? ? ? ? ? ? 5414 ? ? ? ? ? ? ? ? ? ? ? 4.2 1.056 ? ? 0.079 0.034 ? 7  1 0.996 0.999 ? 99.9  ? 0.070 ? ? ? ? ? ? ? ? ? 
3.05 3.49  ? ? ? ? ? ? 5409 ? ? ? ? ? ? ? ? ? ? ? 4.2 1.039 ? ? 0.067 0.028 ? 8  1 0.996 0.999 ? 99.6  ? 0.060 ? ? ? ? ? ? ? ? ? 
3.49 4.39  ? ? ? ? ? ? 5371 ? ? ? ? ? ? ? ? ? ? ? 4.1 1.091 ? ? 0.054 0.023 ? 9  1 0.997 0.999 ? 99.0  ? 0.048 ? ? ? ? ? ? ? ? ? 
4.39 30.00 ? ? ? ? ? ? 5247 ? ? ? ? ? ? ? ? ? ? ? 4.0 1.097 ? ? 0.040 0.018 ? 10 1 0.998 0.999 ? 95.2  ? 0.036 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9IT6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.04 
_refine.ls_d_res_low                             28.62 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     53646 
_refine.ls_number_reflns_R_free                  2783 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.04 
_refine.ls_percent_reflns_R_free                 5.19 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1980 
_refine.ls_R_factor_R_free                       0.2237 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1965 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.49 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.24 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.04 
_refine_hist.d_res_low                        28.62 
_refine_hist.number_atoms_solvent             188 
_refine_hist.number_atoms_total               4716 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4362 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         166 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.917  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 20.521 ? 1781 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.198  ? 739  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 794  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.04 2.07  . . 163 2472 98.00  . . . . 0.2926 . . . . . . . . . . . 0.3293 
'X-RAY DIFFRACTION' 2.07 2.11  . . 146 2530 100.00 . . . . 0.2654 . . . . . . . . . . . 0.3275 
'X-RAY DIFFRACTION' 2.11 2.15  . . 155 2527 100.00 . . . . 0.2543 . . . . . . . . . . . 0.3096 
'X-RAY DIFFRACTION' 2.15 2.19  . . 122 2561 100.00 . . . . 0.2468 . . . . . . . . . . . 0.2726 
'X-RAY DIFFRACTION' 2.19 2.24  . . 142 2572 99.00  . . . . 0.2442 . . . . . . . . . . . 0.3023 
'X-RAY DIFFRACTION' 2.24 2.29  . . 134 2530 99.00  . . . . 0.2706 . . . . . . . . . . . 0.3297 
'X-RAY DIFFRACTION' 2.29 2.35  . . 121 2576 100.00 . . . . 0.2271 . . . . . . . . . . . 0.2597 
'X-RAY DIFFRACTION' 2.35 2.42  . . 110 2584 100.00 . . . . 0.2261 . . . . . . . . . . . 0.2828 
'X-RAY DIFFRACTION' 2.42 2.49  . . 160 2524 100.00 . . . . 0.2107 . . . . . . . . . . . 0.2683 
'X-RAY DIFFRACTION' 2.49 2.57  . . 135 2569 100.00 . . . . 0.2181 . . . . . . . . . . . 0.2291 
'X-RAY DIFFRACTION' 2.57 2.66  . . 137 2545 100.00 . . . . 0.2081 . . . . . . . . . . . 0.2660 
'X-RAY DIFFRACTION' 2.66 2.76  . . 148 2559 100.00 . . . . 0.2247 . . . . . . . . . . . 0.2939 
'X-RAY DIFFRACTION' 2.76 2.89  . . 153 2552 100.00 . . . . 0.2115 . . . . . . . . . . . 0.2366 
'X-RAY DIFFRACTION' 2.89 3.04  . . 144 2572 100.00 . . . . 0.2084 . . . . . . . . . . . 0.2125 
'X-RAY DIFFRACTION' 3.04 3.23  . . 149 2554 100.00 . . . . 0.2146 . . . . . . . . . . . 0.2554 
'X-RAY DIFFRACTION' 3.23 3.48  . . 158 2535 99.00  . . . . 0.1986 . . . . . . . . . . . 0.2266 
'X-RAY DIFFRACTION' 3.48 3.83  . . 120 2577 99.00  . . . . 0.1851 . . . . . . . . . . . 0.2081 
'X-RAY DIFFRACTION' 3.83 4.38  . . 120 2558 99.00  . . . . 0.1628 . . . . . . . . . . . 0.2057 
'X-RAY DIFFRACTION' 4.39 5.52  . . 151 2532 98.00  . . . . 0.1586 . . . . . . . . . . . 0.1689 
'X-RAY DIFFRACTION' 5.52 28.62 . . 115 2434 92.00  . . . . 0.1744 . . . . . . . . . . . 0.1609 
# 
_struct.entry_id                     9IT6 
_struct.title                        'Human MTHFD2 in complex with compound 16g' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9IT6 
_struct_keywords.text            'MTHFD2, methylenetetrahydrofolate dehydrogenase 2, 1C metabolism, mitochondria, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 2 ? 
H N N 3 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MTDC_HUMAN 
_struct_ref.pdbx_db_accession          P13995 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPASISEEELLN
LINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKN
VVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVG
INRVHDPVTAKPKLVGDVDFEGVRQKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKSKELGVATN
;
_struct_ref.pdbx_align_begin           36 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9IT6 A 5 ? 319 ? P13995 36 ? 350 ? 36 350 
2 1 9IT6 B 5 ? 319 ? P13995 36 ? 350 ? 36 350 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9IT6 GLY A 1 ? UNP P13995 ? ? 'expression tag' 32 1 
1 9IT6 SER A 2 ? UNP P13995 ? ? 'expression tag' 33 2 
1 9IT6 HIS A 3 ? UNP P13995 ? ? 'expression tag' 34 3 
1 9IT6 MET A 4 ? UNP P13995 ? ? 'expression tag' 35 4 
2 9IT6 GLY B 1 ? UNP P13995 ? ? 'expression tag' 32 5 
2 9IT6 SER B 2 ? UNP P13995 ? ? 'expression tag' 33 6 
2 9IT6 HIS B 3 ? UNP P13995 ? ? 'expression tag' 34 7 
2 9IT6 MET B 4 ? UNP P13995 ? ? 'expression tag' 35 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6090  ? 
1 MORE         -48   ? 
1 'SSA (A^2)'  21890 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 10  ? SER A 32  ? SER A 41  SER A 63  1 ? 23 
HELX_P HELX_P2  AA2 ASN A 47  ? GLY A 65  ? ASN A 78  GLY A 96  1 ? 19 
HELX_P HELX_P3  AA3 SER A 78  ? ASN A 91  ? SER A 109 ASN A 122 1 ? 14 
HELX_P HELX_P4  AA4 ASP A 109 ? VAL A 117 ? ASP A 140 VAL A 148 1 ? 9  
HELX_P HELX_P5  AA5 SER A 118 ? ASP A 122 ? SER A 149 ASP A 153 5 ? 5  
HELX_P HELX_P6  AA6 HIS A 127 ? LEU A 136 ? HIS A 158 LEU A 167 1 ? 10 
HELX_P HELX_P7  AA7 PRO A 143 ? GLY A 157 ? PRO A 174 GLY A 188 1 ? 15 
HELX_P HELX_P8  AA8 VAL A 174 ? THR A 184 ? VAL A 205 THR A 215 1 ? 11 
HELX_P HELX_P9  AA9 PRO A 205 ? ILE A 214 ? PRO A 236 ILE A 245 1 ? 10 
HELX_P HELX_P10 AB1 THR A 230 ? ILE A 234 ? THR A 261 ILE A 265 5 ? 5  
HELX_P HELX_P11 AB2 ASP A 263 ? ARG A 268 ? ASP A 294 ARG A 299 1 ? 6  
HELX_P HELX_P12 AB3 GLY A 280 ? LYS A 298 ? GLY A 311 LYS A 329 1 ? 19 
HELX_P HELX_P13 AB4 SER B 10  ? SER B 32  ? SER B 41  SER B 63  1 ? 23 
HELX_P HELX_P14 AB5 ASN B 47  ? VAL B 64  ? ASN B 78  VAL B 95  1 ? 18 
HELX_P HELX_P15 AB6 SER B 78  ? ASN B 91  ? SER B 109 ASN B 122 1 ? 14 
HELX_P HELX_P16 AB7 ASP B 109 ? VAL B 117 ? ASP B 140 VAL B 148 1 ? 9  
HELX_P HELX_P17 AB8 SER B 118 ? ASP B 122 ? SER B 149 ASP B 153 5 ? 5  
HELX_P HELX_P18 AB9 HIS B 127 ? LEU B 136 ? HIS B 158 LEU B 167 1 ? 10 
HELX_P HELX_P19 AC1 PRO B 143 ? GLY B 157 ? PRO B 174 GLY B 188 1 ? 15 
HELX_P HELX_P20 AC2 VAL B 174 ? THR B 184 ? VAL B 205 THR B 215 1 ? 11 
HELX_P HELX_P21 AC3 PRO B 205 ? ILE B 214 ? PRO B 236 ILE B 245 1 ? 10 
HELX_P HELX_P22 AC4 THR B 230 ? ILE B 234 ? THR B 261 ILE B 265 5 ? 5  
HELX_P HELX_P23 AC5 ASP B 263 ? ALA B 271 ? ASP B 294 ALA B 302 1 ? 9  
HELX_P HELX_P24 AC6 GLY B 280 ? LYS B 299 ? GLY B 311 LYS B 330 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 102 A . ? LEU 133 A PRO 103 A ? PRO 134 A 1 1.60  
2 VAL 277 A . ? VAL 308 A PRO 278 A ? PRO 309 A 1 -4.51 
3 LEU 102 B . ? LEU 133 B PRO 103 B ? PRO 134 B 1 3.80  
4 VAL 277 B . ? VAL 308 B PRO 278 B ? PRO 309 B 1 -5.65 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 12 ? 
AA2 ? 3  ? 
AA3 ? 3  ? 
AA4 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? parallel      
AA1 2  3  ? parallel      
AA1 3  4  ? parallel      
AA1 4  5  ? parallel      
AA1 5  6  ? parallel      
AA1 6  7  ? anti-parallel 
AA1 7  8  ? parallel      
AA1 8  9  ? parallel      
AA1 9  10 ? parallel      
AA1 10 11 ? parallel      
AA1 11 12 ? parallel      
AA2 1  2  ? parallel      
AA2 2  3  ? parallel      
AA3 1  2  ? parallel      
AA3 2  3  ? parallel      
AA4 1  2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  VAL A 7   ? VAL A 8   ? VAL A 38  VAL A 39  
AA1 2  TYR A 273 ? ILE A 274 ? TYR A 304 ILE A 305 
AA1 3  ALA A 239 ? ASP A 242 ? ALA A 270 ASP A 273 
AA1 4  ILE A 218 ? SER A 221 ? ILE A 249 SER A 252 
AA1 5  ASN A 164 ? ALA A 168 ? ASN A 195 ALA A 199 
AA1 6  THR A 196 ? SER A 200 ? THR A 227 SER A 231 
AA1 7  THR B 196 ? SER B 200 ? THR B 227 SER B 231 
AA1 8  ASN B 164 ? ALA B 168 ? ASN B 195 ALA B 199 
AA1 9  ILE B 218 ? SER B 221 ? ILE B 249 SER B 252 
AA1 10 ALA B 239 ? ASP B 242 ? ALA B 270 ASP B 273 
AA1 11 TYR B 273 ? ILE B 274 ? TYR B 304 ILE B 305 
AA1 12 VAL B 7   ? VAL B 8   ? VAL B 38  VAL B 39  
AA2 1  ASN A 67  ? LYS A 73  ? ASN A 98  LYS A 104 
AA2 2  HIS A 38  ? VAL A 44  ? HIS A 69  VAL A 75  
AA2 3  GLY A 97  ? VAL A 100 ? GLY A 128 VAL A 131 
AA3 1  ASN B 67  ? LYS B 73  ? ASN B 98  LYS B 104 
AA3 2  HIS B 38  ? VAL B 44  ? HIS B 69  VAL B 75  
AA3 3  GLY B 97  ? VAL B 100 ? GLY B 128 VAL B 131 
AA4 1  ASN B 246 ? ARG B 247 ? ASN B 277 ARG B 278 
AA4 2  LEU B 258 ? VAL B 259 ? LEU B 289 VAL B 290 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N VAL A 7   ? N VAL A 38  O ILE A 274 ? O ILE A 305 
AA1 2  3  O TYR A 273 ? O TYR A 304 N VAL A 240 ? N VAL A 271 
AA1 3  4  O ILE A 241 ? O ILE A 272 N VAL A 219 ? N VAL A 250 
AA1 4  5  O ILE A 220 ? O ILE A 251 N VAL A 166 ? N VAL A 197 
AA1 5  6  N VAL A 165 ? N VAL A 196 O THR A 196 ? O THR A 227 
AA1 6  7  N ILE A 199 ? N ILE A 230 O VAL B 197 ? O VAL B 228 
AA1 7  8  O THR B 196 ? O THR B 227 N VAL B 165 ? N VAL B 196 
AA1 8  9  N VAL B 166 ? N VAL B 197 O ILE B 220 ? O ILE B 251 
AA1 9  10 N VAL B 219 ? N VAL B 250 O ILE B 241 ? O ILE B 272 
AA1 10 11 N VAL B 240 ? N VAL B 271 O TYR B 273 ? O TYR B 304 
AA1 11 12 O ILE B 274 ? O ILE B 305 N VAL B 7   ? N VAL B 38  
AA2 1  2  O ILE A 71  ? O ILE A 102 N VAL A 41  ? N VAL A 72  
AA2 2  3  N SER A 40  ? N SER A 71  O GLY A 97  ? O GLY A 128 
AA3 1  2  O ILE B 71  ? O ILE B 102 N VAL B 41  ? N VAL B 72  
AA3 2  3  N SER B 40  ? N SER B 71  O GLY B 97  ? O GLY B 128 
AA4 1  2  N ASN B 246 ? N ASN B 277 O VAL B 259 ? O VAL B 290 
# 
_pdbx_entry_details.entry_id                   9IT6 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 VAL A 205 ? ? -126.24 -68.08  
2 1 HIS A 232 ? ? -160.76 -168.94 
3 1 ASP A 294 ? ? -68.79  93.22   
4 1 VAL B 205 ? ? -125.76 -66.82  
5 1 HIS B 232 ? ? -164.65 -168.62 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 32  ? A GLY 1   
2  1 Y 1 A SER 33  ? A SER 2   
3  1 Y 1 A HIS 34  ? A HIS 3   
4  1 Y 1 A MET 35  ? A MET 4   
5  1 Y 1 A HIS 280 ? A HIS 249 
6  1 Y 1 A ASP 281 ? A ASP 250 
7  1 Y 1 A PRO 282 ? A PRO 251 
8  1 Y 1 A VAL 283 ? A VAL 252 
9  1 Y 1 A THR 284 ? A THR 253 
10 1 Y 1 A ALA 285 ? A ALA 254 
11 1 Y 1 A LYS 286 ? A LYS 255 
12 1 Y 1 A PRO 287 ? A PRO 256 
13 1 Y 1 A ARG 333 ? A ARG 302 
14 1 Y 1 A LEU 334 ? A LEU 303 
15 1 Y 1 A GLU 335 ? A GLU 304 
16 1 Y 1 A GLU 336 ? A GLU 305 
17 1 Y 1 A ARG 337 ? A ARG 306 
18 1 Y 1 A GLU 338 ? A GLU 307 
19 1 Y 1 A VAL 339 ? A VAL 308 
20 1 Y 1 A LEU 340 ? A LEU 309 
21 1 Y 1 A LYS 341 ? A LYS 310 
22 1 Y 1 A SER 342 ? A SER 311 
23 1 Y 1 A LYS 343 ? A LYS 312 
24 1 Y 1 A GLU 344 ? A GLU 313 
25 1 Y 1 A LEU 345 ? A LEU 314 
26 1 Y 1 A GLY 346 ? A GLY 315 
27 1 Y 1 A VAL 347 ? A VAL 316 
28 1 Y 1 A ALA 348 ? A ALA 317 
29 1 Y 1 A THR 349 ? A THR 318 
30 1 Y 1 A ASN 350 ? A ASN 319 
31 1 Y 1 B GLY 32  ? B GLY 1   
32 1 Y 1 B SER 33  ? B SER 2   
33 1 Y 1 B HIS 34  ? B HIS 3   
34 1 Y 1 B MET 35  ? B MET 4   
35 1 Y 1 B ASP 281 ? B ASP 250 
36 1 Y 1 B PRO 282 ? B PRO 251 
37 1 Y 1 B VAL 283 ? B VAL 252 
38 1 Y 1 B THR 284 ? B THR 253 
39 1 Y 1 B ALA 285 ? B ALA 254 
40 1 Y 1 B LYS 286 ? B LYS 255 
41 1 Y 1 B PRO 287 ? B PRO 256 
42 1 Y 1 B ARG 333 ? B ARG 302 
43 1 Y 1 B LEU 334 ? B LEU 303 
44 1 Y 1 B GLU 335 ? B GLU 304 
45 1 Y 1 B GLU 336 ? B GLU 305 
46 1 Y 1 B ARG 337 ? B ARG 306 
47 1 Y 1 B GLU 338 ? B GLU 307 
48 1 Y 1 B VAL 339 ? B VAL 308 
49 1 Y 1 B LEU 340 ? B LEU 309 
50 1 Y 1 B LYS 341 ? B LYS 310 
51 1 Y 1 B SER 342 ? B SER 311 
52 1 Y 1 B LYS 343 ? B LYS 312 
53 1 Y 1 B GLU 344 ? B GLU 313 
54 1 Y 1 B LEU 345 ? B LEU 314 
55 1 Y 1 B GLY 346 ? B GLY 315 
56 1 Y 1 B VAL 347 ? B VAL 316 
57 1 Y 1 B ALA 348 ? B ALA 317 
58 1 Y 1 B THR 349 ? B THR 318 
59 1 Y 1 B ASN 350 ? B ASN 319 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1L24 C10  C  Y N 1   
A1L24 C13  C  Y N 2   
A1L24 C15  C  Y N 3   
A1L24 C17  C  Y N 4   
A1L24 C21  C  N S 5   
A1L24 C22  C  N N 6   
A1L24 C26  C  N N 7   
A1L24 C02  C  N N 8   
A1L24 C04  C  N N 9   
A1L24 C05  C  N N 10  
A1L24 C06  C  N N 11  
A1L24 C08  C  N N 12  
A1L24 C14  C  Y N 13  
A1L24 C16  C  Y N 14  
A1L24 C18  C  N N 15  
A1L24 C23  C  N N 16  
A1L24 C27  C  Y N 17  
A1L24 N01  N  N N 18  
A1L24 N03  N  N N 19  
A1L24 N07  N  N N 20  
A1L24 N09  N  N N 21  
A1L24 N11  N  N N 22  
A1L24 N20  N  N N 23  
A1L24 N28  N  Y N 24  
A1L24 N29  N  Y N 25  
A1L24 N30  N  Y N 26  
A1L24 N31  N  Y N 27  
A1L24 N34  N  N N 28  
A1L24 O12  O  N N 29  
A1L24 O19  O  N N 30  
A1L24 O24  O  N N 31  
A1L24 O25  O  N N 32  
A1L24 O33  O  N N 33  
A1L24 CL32 CL N N 34  
A1L24 H1   H  N N 35  
A1L24 H2   H  N N 36  
A1L24 H3   H  N N 37  
A1L24 H4   H  N N 38  
A1L24 H6   H  N N 39  
A1L24 H7   H  N N 40  
A1L24 H8   H  N N 41  
A1L24 H9   H  N N 42  
A1L24 H10  H  N N 43  
A1L24 H11  H  N N 44  
A1L24 H12  H  N N 45  
A1L24 H13  H  N N 46  
A1L24 H14  H  N N 47  
A1L24 H15  H  N N 48  
A1L24 H16  H  N N 49  
A1L24 H17  H  N N 50  
A1L24 H18  H  N N 51  
A1L24 H5   H  N N 52  
ALA   N    N  N N 53  
ALA   CA   C  N S 54  
ALA   C    C  N N 55  
ALA   O    O  N N 56  
ALA   CB   C  N N 57  
ALA   OXT  O  N N 58  
ALA   H    H  N N 59  
ALA   H2   H  N N 60  
ALA   HA   H  N N 61  
ALA   HB1  H  N N 62  
ALA   HB2  H  N N 63  
ALA   HB3  H  N N 64  
ALA   HXT  H  N N 65  
ARG   N    N  N N 66  
ARG   CA   C  N S 67  
ARG   C    C  N N 68  
ARG   O    O  N N 69  
ARG   CB   C  N N 70  
ARG   CG   C  N N 71  
ARG   CD   C  N N 72  
ARG   NE   N  N N 73  
ARG   CZ   C  N N 74  
ARG   NH1  N  N N 75  
ARG   NH2  N  N N 76  
ARG   OXT  O  N N 77  
ARG   H    H  N N 78  
ARG   H2   H  N N 79  
ARG   HA   H  N N 80  
ARG   HB2  H  N N 81  
ARG   HB3  H  N N 82  
ARG   HG2  H  N N 83  
ARG   HG3  H  N N 84  
ARG   HD2  H  N N 85  
ARG   HD3  H  N N 86  
ARG   HE   H  N N 87  
ARG   HH11 H  N N 88  
ARG   HH12 H  N N 89  
ARG   HH21 H  N N 90  
ARG   HH22 H  N N 91  
ARG   HXT  H  N N 92  
ASN   N    N  N N 93  
ASN   CA   C  N S 94  
ASN   C    C  N N 95  
ASN   O    O  N N 96  
ASN   CB   C  N N 97  
ASN   CG   C  N N 98  
ASN   OD1  O  N N 99  
ASN   ND2  N  N N 100 
ASN   OXT  O  N N 101 
ASN   H    H  N N 102 
ASN   H2   H  N N 103 
ASN   HA   H  N N 104 
ASN   HB2  H  N N 105 
ASN   HB3  H  N N 106 
ASN   HD21 H  N N 107 
ASN   HD22 H  N N 108 
ASN   HXT  H  N N 109 
ASP   N    N  N N 110 
ASP   CA   C  N S 111 
ASP   C    C  N N 112 
ASP   O    O  N N 113 
ASP   CB   C  N N 114 
ASP   CG   C  N N 115 
ASP   OD1  O  N N 116 
ASP   OD2  O  N N 117 
ASP   OXT  O  N N 118 
ASP   H    H  N N 119 
ASP   H2   H  N N 120 
ASP   HA   H  N N 121 
ASP   HB2  H  N N 122 
ASP   HB3  H  N N 123 
ASP   HD2  H  N N 124 
ASP   HXT  H  N N 125 
CYS   N    N  N N 126 
CYS   CA   C  N R 127 
CYS   C    C  N N 128 
CYS   O    O  N N 129 
CYS   CB   C  N N 130 
CYS   SG   S  N N 131 
CYS   OXT  O  N N 132 
CYS   H    H  N N 133 
CYS   H2   H  N N 134 
CYS   HA   H  N N 135 
CYS   HB2  H  N N 136 
CYS   HB3  H  N N 137 
CYS   HG   H  N N 138 
CYS   HXT  H  N N 139 
GLN   N    N  N N 140 
GLN   CA   C  N S 141 
GLN   C    C  N N 142 
GLN   O    O  N N 143 
GLN   CB   C  N N 144 
GLN   CG   C  N N 145 
GLN   CD   C  N N 146 
GLN   OE1  O  N N 147 
GLN   NE2  N  N N 148 
GLN   OXT  O  N N 149 
GLN   H    H  N N 150 
GLN   H2   H  N N 151 
GLN   HA   H  N N 152 
GLN   HB2  H  N N 153 
GLN   HB3  H  N N 154 
GLN   HG2  H  N N 155 
GLN   HG3  H  N N 156 
GLN   HE21 H  N N 157 
GLN   HE22 H  N N 158 
GLN   HXT  H  N N 159 
GLU   N    N  N N 160 
GLU   CA   C  N S 161 
GLU   C    C  N N 162 
GLU   O    O  N N 163 
GLU   CB   C  N N 164 
GLU   CG   C  N N 165 
GLU   CD   C  N N 166 
GLU   OE1  O  N N 167 
GLU   OE2  O  N N 168 
GLU   OXT  O  N N 169 
GLU   H    H  N N 170 
GLU   H2   H  N N 171 
GLU   HA   H  N N 172 
GLU   HB2  H  N N 173 
GLU   HB3  H  N N 174 
GLU   HG2  H  N N 175 
GLU   HG3  H  N N 176 
GLU   HE2  H  N N 177 
GLU   HXT  H  N N 178 
GLY   N    N  N N 179 
GLY   CA   C  N N 180 
GLY   C    C  N N 181 
GLY   O    O  N N 182 
GLY   OXT  O  N N 183 
GLY   H    H  N N 184 
GLY   H2   H  N N 185 
GLY   HA2  H  N N 186 
GLY   HA3  H  N N 187 
GLY   HXT  H  N N 188 
HIS   N    N  N N 189 
HIS   CA   C  N S 190 
HIS   C    C  N N 191 
HIS   O    O  N N 192 
HIS   CB   C  N N 193 
HIS   CG   C  Y N 194 
HIS   ND1  N  Y N 195 
HIS   CD2  C  Y N 196 
HIS   CE1  C  Y N 197 
HIS   NE2  N  Y N 198 
HIS   OXT  O  N N 199 
HIS   H    H  N N 200 
HIS   H2   H  N N 201 
HIS   HA   H  N N 202 
HIS   HB2  H  N N 203 
HIS   HB3  H  N N 204 
HIS   HD1  H  N N 205 
HIS   HD2  H  N N 206 
HIS   HE1  H  N N 207 
HIS   HE2  H  N N 208 
HIS   HXT  H  N N 209 
HOH   O    O  N N 210 
HOH   H1   H  N N 211 
HOH   H2   H  N N 212 
ILE   N    N  N N 213 
ILE   CA   C  N S 214 
ILE   C    C  N N 215 
ILE   O    O  N N 216 
ILE   CB   C  N S 217 
ILE   CG1  C  N N 218 
ILE   CG2  C  N N 219 
ILE   CD1  C  N N 220 
ILE   OXT  O  N N 221 
ILE   H    H  N N 222 
ILE   H2   H  N N 223 
ILE   HA   H  N N 224 
ILE   HB   H  N N 225 
ILE   HG12 H  N N 226 
ILE   HG13 H  N N 227 
ILE   HG21 H  N N 228 
ILE   HG22 H  N N 229 
ILE   HG23 H  N N 230 
ILE   HD11 H  N N 231 
ILE   HD12 H  N N 232 
ILE   HD13 H  N N 233 
ILE   HXT  H  N N 234 
LEU   N    N  N N 235 
LEU   CA   C  N S 236 
LEU   C    C  N N 237 
LEU   O    O  N N 238 
LEU   CB   C  N N 239 
LEU   CG   C  N N 240 
LEU   CD1  C  N N 241 
LEU   CD2  C  N N 242 
LEU   OXT  O  N N 243 
LEU   H    H  N N 244 
LEU   H2   H  N N 245 
LEU   HA   H  N N 246 
LEU   HB2  H  N N 247 
LEU   HB3  H  N N 248 
LEU   HG   H  N N 249 
LEU   HD11 H  N N 250 
LEU   HD12 H  N N 251 
LEU   HD13 H  N N 252 
LEU   HD21 H  N N 253 
LEU   HD22 H  N N 254 
LEU   HD23 H  N N 255 
LEU   HXT  H  N N 256 
LYS   N    N  N N 257 
LYS   CA   C  N S 258 
LYS   C    C  N N 259 
LYS   O    O  N N 260 
LYS   CB   C  N N 261 
LYS   CG   C  N N 262 
LYS   CD   C  N N 263 
LYS   CE   C  N N 264 
LYS   NZ   N  N N 265 
LYS   OXT  O  N N 266 
LYS   H    H  N N 267 
LYS   H2   H  N N 268 
LYS   HA   H  N N 269 
LYS   HB2  H  N N 270 
LYS   HB3  H  N N 271 
LYS   HG2  H  N N 272 
LYS   HG3  H  N N 273 
LYS   HD2  H  N N 274 
LYS   HD3  H  N N 275 
LYS   HE2  H  N N 276 
LYS   HE3  H  N N 277 
LYS   HZ1  H  N N 278 
LYS   HZ2  H  N N 279 
LYS   HZ3  H  N N 280 
LYS   HXT  H  N N 281 
MET   N    N  N N 282 
MET   CA   C  N S 283 
MET   C    C  N N 284 
MET   O    O  N N 285 
MET   CB   C  N N 286 
MET   CG   C  N N 287 
MET   SD   S  N N 288 
MET   CE   C  N N 289 
MET   OXT  O  N N 290 
MET   H    H  N N 291 
MET   H2   H  N N 292 
MET   HA   H  N N 293 
MET   HB2  H  N N 294 
MET   HB3  H  N N 295 
MET   HG2  H  N N 296 
MET   HG3  H  N N 297 
MET   HE1  H  N N 298 
MET   HE2  H  N N 299 
MET   HE3  H  N N 300 
MET   HXT  H  N N 301 
NAD   PA   P  N S 302 
NAD   O1A  O  N N 303 
NAD   O2A  O  N N 304 
NAD   O5B  O  N N 305 
NAD   C5B  C  N N 306 
NAD   C4B  C  N R 307 
NAD   O4B  O  N N 308 
NAD   C3B  C  N S 309 
NAD   O3B  O  N N 310 
NAD   C2B  C  N R 311 
NAD   O2B  O  N N 312 
NAD   C1B  C  N R 313 
NAD   N9A  N  Y N 314 
NAD   C8A  C  Y N 315 
NAD   N7A  N  Y N 316 
NAD   C5A  C  Y N 317 
NAD   C6A  C  Y N 318 
NAD   N6A  N  N N 319 
NAD   N1A  N  Y N 320 
NAD   C2A  C  Y N 321 
NAD   N3A  N  Y N 322 
NAD   C4A  C  Y N 323 
NAD   O3   O  N N 324 
NAD   PN   P  N N 325 
NAD   O1N  O  N N 326 
NAD   O2N  O  N N 327 
NAD   O5D  O  N N 328 
NAD   C5D  C  N N 329 
NAD   C4D  C  N R 330 
NAD   O4D  O  N N 331 
NAD   C3D  C  N S 332 
NAD   O3D  O  N N 333 
NAD   C2D  C  N R 334 
NAD   O2D  O  N N 335 
NAD   C1D  C  N R 336 
NAD   N1N  N  Y N 337 
NAD   C2N  C  Y N 338 
NAD   C3N  C  Y N 339 
NAD   C7N  C  N N 340 
NAD   O7N  O  N N 341 
NAD   N7N  N  N N 342 
NAD   C4N  C  Y N 343 
NAD   C5N  C  Y N 344 
NAD   C6N  C  Y N 345 
NAD   HOA2 H  N N 346 
NAD   H51A H  N N 347 
NAD   H52A H  N N 348 
NAD   H4B  H  N N 349 
NAD   H3B  H  N N 350 
NAD   HO3A H  N N 351 
NAD   H2B  H  N N 352 
NAD   HO2A H  N N 353 
NAD   H1B  H  N N 354 
NAD   H8A  H  N N 355 
NAD   H61A H  N N 356 
NAD   H62A H  N N 357 
NAD   H2A  H  N N 358 
NAD   H51N H  N N 359 
NAD   H52N H  N N 360 
NAD   H4D  H  N N 361 
NAD   H3D  H  N N 362 
NAD   HO3N H  N N 363 
NAD   H2D  H  N N 364 
NAD   HO2N H  N N 365 
NAD   H1D  H  N N 366 
NAD   H2N  H  N N 367 
NAD   H71N H  N N 368 
NAD   H72N H  N N 369 
NAD   H4N  H  N N 370 
NAD   H5N  H  N N 371 
NAD   H6N  H  N N 372 
PHE   N    N  N N 373 
PHE   CA   C  N S 374 
PHE   C    C  N N 375 
PHE   O    O  N N 376 
PHE   CB   C  N N 377 
PHE   CG   C  Y N 378 
PHE   CD1  C  Y N 379 
PHE   CD2  C  Y N 380 
PHE   CE1  C  Y N 381 
PHE   CE2  C  Y N 382 
PHE   CZ   C  Y N 383 
PHE   OXT  O  N N 384 
PHE   H    H  N N 385 
PHE   H2   H  N N 386 
PHE   HA   H  N N 387 
PHE   HB2  H  N N 388 
PHE   HB3  H  N N 389 
PHE   HD1  H  N N 390 
PHE   HD2  H  N N 391 
PHE   HE1  H  N N 392 
PHE   HE2  H  N N 393 
PHE   HZ   H  N N 394 
PHE   HXT  H  N N 395 
PO4   P    P  N N 396 
PO4   O1   O  N N 397 
PO4   O2   O  N N 398 
PO4   O3   O  N N 399 
PO4   O4   O  N N 400 
PRO   N    N  N N 401 
PRO   CA   C  N S 402 
PRO   C    C  N N 403 
PRO   O    O  N N 404 
PRO   CB   C  N N 405 
PRO   CG   C  N N 406 
PRO   CD   C  N N 407 
PRO   OXT  O  N N 408 
PRO   H    H  N N 409 
PRO   HA   H  N N 410 
PRO   HB2  H  N N 411 
PRO   HB3  H  N N 412 
PRO   HG2  H  N N 413 
PRO   HG3  H  N N 414 
PRO   HD2  H  N N 415 
PRO   HD3  H  N N 416 
PRO   HXT  H  N N 417 
SER   N    N  N N 418 
SER   CA   C  N S 419 
SER   C    C  N N 420 
SER   O    O  N N 421 
SER   CB   C  N N 422 
SER   OG   O  N N 423 
SER   OXT  O  N N 424 
SER   H    H  N N 425 
SER   H2   H  N N 426 
SER   HA   H  N N 427 
SER   HB2  H  N N 428 
SER   HB3  H  N N 429 
SER   HG   H  N N 430 
SER   HXT  H  N N 431 
THR   N    N  N N 432 
THR   CA   C  N S 433 
THR   C    C  N N 434 
THR   O    O  N N 435 
THR   CB   C  N R 436 
THR   OG1  O  N N 437 
THR   CG2  C  N N 438 
THR   OXT  O  N N 439 
THR   H    H  N N 440 
THR   H2   H  N N 441 
THR   HA   H  N N 442 
THR   HB   H  N N 443 
THR   HG1  H  N N 444 
THR   HG21 H  N N 445 
THR   HG22 H  N N 446 
THR   HG23 H  N N 447 
THR   HXT  H  N N 448 
TRP   N    N  N N 449 
TRP   CA   C  N S 450 
TRP   C    C  N N 451 
TRP   O    O  N N 452 
TRP   CB   C  N N 453 
TRP   CG   C  Y N 454 
TRP   CD1  C  Y N 455 
TRP   CD2  C  Y N 456 
TRP   NE1  N  Y N 457 
TRP   CE2  C  Y N 458 
TRP   CE3  C  Y N 459 
TRP   CZ2  C  Y N 460 
TRP   CZ3  C  Y N 461 
TRP   CH2  C  Y N 462 
TRP   OXT  O  N N 463 
TRP   H    H  N N 464 
TRP   H2   H  N N 465 
TRP   HA   H  N N 466 
TRP   HB2  H  N N 467 
TRP   HB3  H  N N 468 
TRP   HD1  H  N N 469 
TRP   HE1  H  N N 470 
TRP   HE3  H  N N 471 
TRP   HZ2  H  N N 472 
TRP   HZ3  H  N N 473 
TRP   HH2  H  N N 474 
TRP   HXT  H  N N 475 
TYR   N    N  N N 476 
TYR   CA   C  N S 477 
TYR   C    C  N N 478 
TYR   O    O  N N 479 
TYR   CB   C  N N 480 
TYR   CG   C  Y N 481 
TYR   CD1  C  Y N 482 
TYR   CD2  C  Y N 483 
TYR   CE1  C  Y N 484 
TYR   CE2  C  Y N 485 
TYR   CZ   C  Y N 486 
TYR   OH   O  N N 487 
TYR   OXT  O  N N 488 
TYR   H    H  N N 489 
TYR   H2   H  N N 490 
TYR   HA   H  N N 491 
TYR   HB2  H  N N 492 
TYR   HB3  H  N N 493 
TYR   HD1  H  N N 494 
TYR   HD2  H  N N 495 
TYR   HE1  H  N N 496 
TYR   HE2  H  N N 497 
TYR   HH   H  N N 498 
TYR   HXT  H  N N 499 
VAL   N    N  N N 500 
VAL   CA   C  N S 501 
VAL   C    C  N N 502 
VAL   O    O  N N 503 
VAL   CB   C  N N 504 
VAL   CG1  C  N N 505 
VAL   CG2  C  N N 506 
VAL   OXT  O  N N 507 
VAL   H    H  N N 508 
VAL   H2   H  N N 509 
VAL   HA   H  N N 510 
VAL   HB   H  N N 511 
VAL   HG11 H  N N 512 
VAL   HG12 H  N N 513 
VAL   HG13 H  N N 514 
VAL   HG21 H  N N 515 
VAL   HG22 H  N N 516 
VAL   HG23 H  N N 517 
VAL   HXT  H  N N 518 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1L24 O25 C22  doub N N 1   
A1L24 N31 N30  sing Y N 2   
A1L24 N31 C27  doub Y N 3   
A1L24 N30 N29  doub Y N 4   
A1L24 C22 C21  sing N N 5   
A1L24 C22 O24  sing N N 6   
A1L24 C23 C21  sing N N 7   
A1L24 C23 C26  sing N N 8   
A1L24 C21 N20  sing N N 9   
A1L24 C27 C26  sing N N 10  
A1L24 C27 N28  sing Y N 11  
A1L24 N29 N28  sing Y N 12  
A1L24 N20 C18  sing N N 13  
A1L24 O19 C18  doub N N 14  
A1L24 C18 C15  sing N N 15  
A1L24 C15 C16  sing Y N 16  
A1L24 C15 C14  doub Y N 17  
A1L24 C16 C17  doub Y N 18  
A1L24 C14 C13  sing Y N 19  
A1L24 C17 C10  sing Y N 20  
A1L24 C17 CL32 sing N N 21  
A1L24 C13 C10  doub Y N 22  
A1L24 C10 N09  sing N N 23  
A1L24 N09 C08  sing N N 24  
A1L24 O12 C08  doub N N 25  
A1L24 C08 N07  sing N N 26  
A1L24 N07 C05  sing N N 27  
A1L24 O33 C06  doub N N 28  
A1L24 C06 C05  sing N N 29  
A1L24 C06 N01  sing N N 30  
A1L24 C05 C04  doub N N 31  
A1L24 N01 C02  sing N N 32  
A1L24 C04 N11  sing N N 33  
A1L24 C04 N03  sing N N 34  
A1L24 C02 N03  doub N N 35  
A1L24 C02 N34  sing N N 36  
A1L24 C13 H1   sing N N 37  
A1L24 C21 H2   sing N N 38  
A1L24 C26 H3   sing N N 39  
A1L24 C26 H4   sing N N 40  
A1L24 C14 H6   sing N N 41  
A1L24 C16 H7   sing N N 42  
A1L24 C23 H8   sing N N 43  
A1L24 C23 H9   sing N N 44  
A1L24 N07 H10  sing N N 45  
A1L24 N09 H11  sing N N 46  
A1L24 N11 H12  sing N N 47  
A1L24 N11 H13  sing N N 48  
A1L24 N20 H14  sing N N 49  
A1L24 N28 H15  sing N N 50  
A1L24 N34 H16  sing N N 51  
A1L24 N34 H17  sing N N 52  
A1L24 O24 H18  sing N N 53  
A1L24 N01 H5   sing N N 54  
ALA   N   CA   sing N N 55  
ALA   N   H    sing N N 56  
ALA   N   H2   sing N N 57  
ALA   CA  C    sing N N 58  
ALA   CA  CB   sing N N 59  
ALA   CA  HA   sing N N 60  
ALA   C   O    doub N N 61  
ALA   C   OXT  sing N N 62  
ALA   CB  HB1  sing N N 63  
ALA   CB  HB2  sing N N 64  
ALA   CB  HB3  sing N N 65  
ALA   OXT HXT  sing N N 66  
ARG   N   CA   sing N N 67  
ARG   N   H    sing N N 68  
ARG   N   H2   sing N N 69  
ARG   CA  C    sing N N 70  
ARG   CA  CB   sing N N 71  
ARG   CA  HA   sing N N 72  
ARG   C   O    doub N N 73  
ARG   C   OXT  sing N N 74  
ARG   CB  CG   sing N N 75  
ARG   CB  HB2  sing N N 76  
ARG   CB  HB3  sing N N 77  
ARG   CG  CD   sing N N 78  
ARG   CG  HG2  sing N N 79  
ARG   CG  HG3  sing N N 80  
ARG   CD  NE   sing N N 81  
ARG   CD  HD2  sing N N 82  
ARG   CD  HD3  sing N N 83  
ARG   NE  CZ   sing N N 84  
ARG   NE  HE   sing N N 85  
ARG   CZ  NH1  sing N N 86  
ARG   CZ  NH2  doub N N 87  
ARG   NH1 HH11 sing N N 88  
ARG   NH1 HH12 sing N N 89  
ARG   NH2 HH21 sing N N 90  
ARG   NH2 HH22 sing N N 91  
ARG   OXT HXT  sing N N 92  
ASN   N   CA   sing N N 93  
ASN   N   H    sing N N 94  
ASN   N   H2   sing N N 95  
ASN   CA  C    sing N N 96  
ASN   CA  CB   sing N N 97  
ASN   CA  HA   sing N N 98  
ASN   C   O    doub N N 99  
ASN   C   OXT  sing N N 100 
ASN   CB  CG   sing N N 101 
ASN   CB  HB2  sing N N 102 
ASN   CB  HB3  sing N N 103 
ASN   CG  OD1  doub N N 104 
ASN   CG  ND2  sing N N 105 
ASN   ND2 HD21 sing N N 106 
ASN   ND2 HD22 sing N N 107 
ASN   OXT HXT  sing N N 108 
ASP   N   CA   sing N N 109 
ASP   N   H    sing N N 110 
ASP   N   H2   sing N N 111 
ASP   CA  C    sing N N 112 
ASP   CA  CB   sing N N 113 
ASP   CA  HA   sing N N 114 
ASP   C   O    doub N N 115 
ASP   C   OXT  sing N N 116 
ASP   CB  CG   sing N N 117 
ASP   CB  HB2  sing N N 118 
ASP   CB  HB3  sing N N 119 
ASP   CG  OD1  doub N N 120 
ASP   CG  OD2  sing N N 121 
ASP   OD2 HD2  sing N N 122 
ASP   OXT HXT  sing N N 123 
CYS   N   CA   sing N N 124 
CYS   N   H    sing N N 125 
CYS   N   H2   sing N N 126 
CYS   CA  C    sing N N 127 
CYS   CA  CB   sing N N 128 
CYS   CA  HA   sing N N 129 
CYS   C   O    doub N N 130 
CYS   C   OXT  sing N N 131 
CYS   CB  SG   sing N N 132 
CYS   CB  HB2  sing N N 133 
CYS   CB  HB3  sing N N 134 
CYS   SG  HG   sing N N 135 
CYS   OXT HXT  sing N N 136 
GLN   N   CA   sing N N 137 
GLN   N   H    sing N N 138 
GLN   N   H2   sing N N 139 
GLN   CA  C    sing N N 140 
GLN   CA  CB   sing N N 141 
GLN   CA  HA   sing N N 142 
GLN   C   O    doub N N 143 
GLN   C   OXT  sing N N 144 
GLN   CB  CG   sing N N 145 
GLN   CB  HB2  sing N N 146 
GLN   CB  HB3  sing N N 147 
GLN   CG  CD   sing N N 148 
GLN   CG  HG2  sing N N 149 
GLN   CG  HG3  sing N N 150 
GLN   CD  OE1  doub N N 151 
GLN   CD  NE2  sing N N 152 
GLN   NE2 HE21 sing N N 153 
GLN   NE2 HE22 sing N N 154 
GLN   OXT HXT  sing N N 155 
GLU   N   CA   sing N N 156 
GLU   N   H    sing N N 157 
GLU   N   H2   sing N N 158 
GLU   CA  C    sing N N 159 
GLU   CA  CB   sing N N 160 
GLU   CA  HA   sing N N 161 
GLU   C   O    doub N N 162 
GLU   C   OXT  sing N N 163 
GLU   CB  CG   sing N N 164 
GLU   CB  HB2  sing N N 165 
GLU   CB  HB3  sing N N 166 
GLU   CG  CD   sing N N 167 
GLU   CG  HG2  sing N N 168 
GLU   CG  HG3  sing N N 169 
GLU   CD  OE1  doub N N 170 
GLU   CD  OE2  sing N N 171 
GLU   OE2 HE2  sing N N 172 
GLU   OXT HXT  sing N N 173 
GLY   N   CA   sing N N 174 
GLY   N   H    sing N N 175 
GLY   N   H2   sing N N 176 
GLY   CA  C    sing N N 177 
GLY   CA  HA2  sing N N 178 
GLY   CA  HA3  sing N N 179 
GLY   C   O    doub N N 180 
GLY   C   OXT  sing N N 181 
GLY   OXT HXT  sing N N 182 
HIS   N   CA   sing N N 183 
HIS   N   H    sing N N 184 
HIS   N   H2   sing N N 185 
HIS   CA  C    sing N N 186 
HIS   CA  CB   sing N N 187 
HIS   CA  HA   sing N N 188 
HIS   C   O    doub N N 189 
HIS   C   OXT  sing N N 190 
HIS   CB  CG   sing N N 191 
HIS   CB  HB2  sing N N 192 
HIS   CB  HB3  sing N N 193 
HIS   CG  ND1  sing Y N 194 
HIS   CG  CD2  doub Y N 195 
HIS   ND1 CE1  doub Y N 196 
HIS   ND1 HD1  sing N N 197 
HIS   CD2 NE2  sing Y N 198 
HIS   CD2 HD2  sing N N 199 
HIS   CE1 NE2  sing Y N 200 
HIS   CE1 HE1  sing N N 201 
HIS   NE2 HE2  sing N N 202 
HIS   OXT HXT  sing N N 203 
HOH   O   H1   sing N N 204 
HOH   O   H2   sing N N 205 
ILE   N   CA   sing N N 206 
ILE   N   H    sing N N 207 
ILE   N   H2   sing N N 208 
ILE   CA  C    sing N N 209 
ILE   CA  CB   sing N N 210 
ILE   CA  HA   sing N N 211 
ILE   C   O    doub N N 212 
ILE   C   OXT  sing N N 213 
ILE   CB  CG1  sing N N 214 
ILE   CB  CG2  sing N N 215 
ILE   CB  HB   sing N N 216 
ILE   CG1 CD1  sing N N 217 
ILE   CG1 HG12 sing N N 218 
ILE   CG1 HG13 sing N N 219 
ILE   CG2 HG21 sing N N 220 
ILE   CG2 HG22 sing N N 221 
ILE   CG2 HG23 sing N N 222 
ILE   CD1 HD11 sing N N 223 
ILE   CD1 HD12 sing N N 224 
ILE   CD1 HD13 sing N N 225 
ILE   OXT HXT  sing N N 226 
LEU   N   CA   sing N N 227 
LEU   N   H    sing N N 228 
LEU   N   H2   sing N N 229 
LEU   CA  C    sing N N 230 
LEU   CA  CB   sing N N 231 
LEU   CA  HA   sing N N 232 
LEU   C   O    doub N N 233 
LEU   C   OXT  sing N N 234 
LEU   CB  CG   sing N N 235 
LEU   CB  HB2  sing N N 236 
LEU   CB  HB3  sing N N 237 
LEU   CG  CD1  sing N N 238 
LEU   CG  CD2  sing N N 239 
LEU   CG  HG   sing N N 240 
LEU   CD1 HD11 sing N N 241 
LEU   CD1 HD12 sing N N 242 
LEU   CD1 HD13 sing N N 243 
LEU   CD2 HD21 sing N N 244 
LEU   CD2 HD22 sing N N 245 
LEU   CD2 HD23 sing N N 246 
LEU   OXT HXT  sing N N 247 
LYS   N   CA   sing N N 248 
LYS   N   H    sing N N 249 
LYS   N   H2   sing N N 250 
LYS   CA  C    sing N N 251 
LYS   CA  CB   sing N N 252 
LYS   CA  HA   sing N N 253 
LYS   C   O    doub N N 254 
LYS   C   OXT  sing N N 255 
LYS   CB  CG   sing N N 256 
LYS   CB  HB2  sing N N 257 
LYS   CB  HB3  sing N N 258 
LYS   CG  CD   sing N N 259 
LYS   CG  HG2  sing N N 260 
LYS   CG  HG3  sing N N 261 
LYS   CD  CE   sing N N 262 
LYS   CD  HD2  sing N N 263 
LYS   CD  HD3  sing N N 264 
LYS   CE  NZ   sing N N 265 
LYS   CE  HE2  sing N N 266 
LYS   CE  HE3  sing N N 267 
LYS   NZ  HZ1  sing N N 268 
LYS   NZ  HZ2  sing N N 269 
LYS   NZ  HZ3  sing N N 270 
LYS   OXT HXT  sing N N 271 
MET   N   CA   sing N N 272 
MET   N   H    sing N N 273 
MET   N   H2   sing N N 274 
MET   CA  C    sing N N 275 
MET   CA  CB   sing N N 276 
MET   CA  HA   sing N N 277 
MET   C   O    doub N N 278 
MET   C   OXT  sing N N 279 
MET   CB  CG   sing N N 280 
MET   CB  HB2  sing N N 281 
MET   CB  HB3  sing N N 282 
MET   CG  SD   sing N N 283 
MET   CG  HG2  sing N N 284 
MET   CG  HG3  sing N N 285 
MET   SD  CE   sing N N 286 
MET   CE  HE1  sing N N 287 
MET   CE  HE2  sing N N 288 
MET   CE  HE3  sing N N 289 
MET   OXT HXT  sing N N 290 
NAD   PA  O1A  doub N N 291 
NAD   PA  O2A  sing N N 292 
NAD   PA  O5B  sing N N 293 
NAD   PA  O3   sing N N 294 
NAD   O2A HOA2 sing N N 295 
NAD   O5B C5B  sing N N 296 
NAD   C5B C4B  sing N N 297 
NAD   C5B H51A sing N N 298 
NAD   C5B H52A sing N N 299 
NAD   C4B O4B  sing N N 300 
NAD   C4B C3B  sing N N 301 
NAD   C4B H4B  sing N N 302 
NAD   O4B C1B  sing N N 303 
NAD   C3B O3B  sing N N 304 
NAD   C3B C2B  sing N N 305 
NAD   C3B H3B  sing N N 306 
NAD   O3B HO3A sing N N 307 
NAD   C2B O2B  sing N N 308 
NAD   C2B C1B  sing N N 309 
NAD   C2B H2B  sing N N 310 
NAD   O2B HO2A sing N N 311 
NAD   C1B N9A  sing N N 312 
NAD   C1B H1B  sing N N 313 
NAD   N9A C8A  sing Y N 314 
NAD   N9A C4A  sing Y N 315 
NAD   C8A N7A  doub Y N 316 
NAD   C8A H8A  sing N N 317 
NAD   N7A C5A  sing Y N 318 
NAD   C5A C6A  sing Y N 319 
NAD   C5A C4A  doub Y N 320 
NAD   C6A N6A  sing N N 321 
NAD   C6A N1A  doub Y N 322 
NAD   N6A H61A sing N N 323 
NAD   N6A H62A sing N N 324 
NAD   N1A C2A  sing Y N 325 
NAD   C2A N3A  doub Y N 326 
NAD   C2A H2A  sing N N 327 
NAD   N3A C4A  sing Y N 328 
NAD   O3  PN   sing N N 329 
NAD   PN  O1N  doub N N 330 
NAD   PN  O2N  sing N N 331 
NAD   PN  O5D  sing N N 332 
NAD   O5D C5D  sing N N 333 
NAD   C5D C4D  sing N N 334 
NAD   C5D H51N sing N N 335 
NAD   C5D H52N sing N N 336 
NAD   C4D O4D  sing N N 337 
NAD   C4D C3D  sing N N 338 
NAD   C4D H4D  sing N N 339 
NAD   O4D C1D  sing N N 340 
NAD   C3D O3D  sing N N 341 
NAD   C3D C2D  sing N N 342 
NAD   C3D H3D  sing N N 343 
NAD   O3D HO3N sing N N 344 
NAD   C2D O2D  sing N N 345 
NAD   C2D C1D  sing N N 346 
NAD   C2D H2D  sing N N 347 
NAD   O2D HO2N sing N N 348 
NAD   C1D N1N  sing N N 349 
NAD   C1D H1D  sing N N 350 
NAD   N1N C2N  sing Y N 351 
NAD   N1N C6N  doub Y N 352 
NAD   C2N C3N  doub Y N 353 
NAD   C2N H2N  sing N N 354 
NAD   C3N C7N  sing N N 355 
NAD   C3N C4N  sing Y N 356 
NAD   C7N O7N  doub N N 357 
NAD   C7N N7N  sing N N 358 
NAD   N7N H71N sing N N 359 
NAD   N7N H72N sing N N 360 
NAD   C4N C5N  doub Y N 361 
NAD   C4N H4N  sing N N 362 
NAD   C5N C6N  sing Y N 363 
NAD   C5N H5N  sing N N 364 
NAD   C6N H6N  sing N N 365 
PHE   N   CA   sing N N 366 
PHE   N   H    sing N N 367 
PHE   N   H2   sing N N 368 
PHE   CA  C    sing N N 369 
PHE   CA  CB   sing N N 370 
PHE   CA  HA   sing N N 371 
PHE   C   O    doub N N 372 
PHE   C   OXT  sing N N 373 
PHE   CB  CG   sing N N 374 
PHE   CB  HB2  sing N N 375 
PHE   CB  HB3  sing N N 376 
PHE   CG  CD1  doub Y N 377 
PHE   CG  CD2  sing Y N 378 
PHE   CD1 CE1  sing Y N 379 
PHE   CD1 HD1  sing N N 380 
PHE   CD2 CE2  doub Y N 381 
PHE   CD2 HD2  sing N N 382 
PHE   CE1 CZ   doub Y N 383 
PHE   CE1 HE1  sing N N 384 
PHE   CE2 CZ   sing Y N 385 
PHE   CE2 HE2  sing N N 386 
PHE   CZ  HZ   sing N N 387 
PHE   OXT HXT  sing N N 388 
PO4   P   O1   doub N N 389 
PO4   P   O2   sing N N 390 
PO4   P   O3   sing N N 391 
PO4   P   O4   sing N N 392 
PRO   N   CA   sing N N 393 
PRO   N   CD   sing N N 394 
PRO   N   H    sing N N 395 
PRO   CA  C    sing N N 396 
PRO   CA  CB   sing N N 397 
PRO   CA  HA   sing N N 398 
PRO   C   O    doub N N 399 
PRO   C   OXT  sing N N 400 
PRO   CB  CG   sing N N 401 
PRO   CB  HB2  sing N N 402 
PRO   CB  HB3  sing N N 403 
PRO   CG  CD   sing N N 404 
PRO   CG  HG2  sing N N 405 
PRO   CG  HG3  sing N N 406 
PRO   CD  HD2  sing N N 407 
PRO   CD  HD3  sing N N 408 
PRO   OXT HXT  sing N N 409 
SER   N   CA   sing N N 410 
SER   N   H    sing N N 411 
SER   N   H2   sing N N 412 
SER   CA  C    sing N N 413 
SER   CA  CB   sing N N 414 
SER   CA  HA   sing N N 415 
SER   C   O    doub N N 416 
SER   C   OXT  sing N N 417 
SER   CB  OG   sing N N 418 
SER   CB  HB2  sing N N 419 
SER   CB  HB3  sing N N 420 
SER   OG  HG   sing N N 421 
SER   OXT HXT  sing N N 422 
THR   N   CA   sing N N 423 
THR   N   H    sing N N 424 
THR   N   H2   sing N N 425 
THR   CA  C    sing N N 426 
THR   CA  CB   sing N N 427 
THR   CA  HA   sing N N 428 
THR   C   O    doub N N 429 
THR   C   OXT  sing N N 430 
THR   CB  OG1  sing N N 431 
THR   CB  CG2  sing N N 432 
THR   CB  HB   sing N N 433 
THR   OG1 HG1  sing N N 434 
THR   CG2 HG21 sing N N 435 
THR   CG2 HG22 sing N N 436 
THR   CG2 HG23 sing N N 437 
THR   OXT HXT  sing N N 438 
TRP   N   CA   sing N N 439 
TRP   N   H    sing N N 440 
TRP   N   H2   sing N N 441 
TRP   CA  C    sing N N 442 
TRP   CA  CB   sing N N 443 
TRP   CA  HA   sing N N 444 
TRP   C   O    doub N N 445 
TRP   C   OXT  sing N N 446 
TRP   CB  CG   sing N N 447 
TRP   CB  HB2  sing N N 448 
TRP   CB  HB3  sing N N 449 
TRP   CG  CD1  doub Y N 450 
TRP   CG  CD2  sing Y N 451 
TRP   CD1 NE1  sing Y N 452 
TRP   CD1 HD1  sing N N 453 
TRP   CD2 CE2  doub Y N 454 
TRP   CD2 CE3  sing Y N 455 
TRP   NE1 CE2  sing Y N 456 
TRP   NE1 HE1  sing N N 457 
TRP   CE2 CZ2  sing Y N 458 
TRP   CE3 CZ3  doub Y N 459 
TRP   CE3 HE3  sing N N 460 
TRP   CZ2 CH2  doub Y N 461 
TRP   CZ2 HZ2  sing N N 462 
TRP   CZ3 CH2  sing Y N 463 
TRP   CZ3 HZ3  sing N N 464 
TRP   CH2 HH2  sing N N 465 
TRP   OXT HXT  sing N N 466 
TYR   N   CA   sing N N 467 
TYR   N   H    sing N N 468 
TYR   N   H2   sing N N 469 
TYR   CA  C    sing N N 470 
TYR   CA  CB   sing N N 471 
TYR   CA  HA   sing N N 472 
TYR   C   O    doub N N 473 
TYR   C   OXT  sing N N 474 
TYR   CB  CG   sing N N 475 
TYR   CB  HB2  sing N N 476 
TYR   CB  HB3  sing N N 477 
TYR   CG  CD1  doub Y N 478 
TYR   CG  CD2  sing Y N 479 
TYR   CD1 CE1  sing Y N 480 
TYR   CD1 HD1  sing N N 481 
TYR   CD2 CE2  doub Y N 482 
TYR   CD2 HD2  sing N N 483 
TYR   CE1 CZ   doub Y N 484 
TYR   CE1 HE1  sing N N 485 
TYR   CE2 CZ   sing Y N 486 
TYR   CE2 HE2  sing N N 487 
TYR   CZ  OH   sing N N 488 
TYR   OH  HH   sing N N 489 
TYR   OXT HXT  sing N N 490 
VAL   N   CA   sing N N 491 
VAL   N   H    sing N N 492 
VAL   N   H2   sing N N 493 
VAL   CA  C    sing N N 494 
VAL   CA  CB   sing N N 495 
VAL   CA  HA   sing N N 496 
VAL   C   O    doub N N 497 
VAL   C   OXT  sing N N 498 
VAL   CB  CG1  sing N N 499 
VAL   CB  CG2  sing N N 500 
VAL   CB  HB   sing N N 501 
VAL   CG1 HG11 sing N N 502 
VAL   CG1 HG12 sing N N 503 
VAL   CG1 HG13 sing N N 504 
VAL   CG2 HG21 sing N N 505 
VAL   CG2 HG22 sing N N 506 
VAL   CG2 HG23 sing N N 507 
VAL   OXT HXT  sing N N 508 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5TC4 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9IT6 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.008707 
_atom_sites.fract_transf_matrix[1][2]   0.005027 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010054 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.008817 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . GLU   A 1 5   ? -36.224 9.061  27.627  1.00 63.15 ? 36  GLU   A N    1 
ATOM   2    C  CA   . GLU   A 1 5   ? -37.422 9.716  27.100  1.00 64.19 ? 36  GLU   A CA   1 
ATOM   3    C  C    . GLU   A 1 5   ? -37.358 11.238 27.284  1.00 63.07 ? 36  GLU   A C    1 
ATOM   4    O  O    . GLU   A 1 5   ? -36.746 11.727 28.237  1.00 62.03 ? 36  GLU   A O    1 
ATOM   5    C  CB   . GLU   A 1 5   ? -38.675 9.152  27.772  1.00 68.10 ? 36  GLU   A CB   1 
ATOM   6    C  CG   . GLU   A 1 5   ? -39.982 9.697  27.218  1.00 69.14 ? 36  GLU   A CG   1 
ATOM   7    C  CD   . GLU   A 1 5   ? -41.198 9.035  27.836  1.00 78.49 ? 36  GLU   A CD   1 
ATOM   8    O  OE1  . GLU   A 1 5   ? -42.262 9.689  27.907  1.00 80.92 ? 36  GLU   A OE1  1 
ATOM   9    O  OE2  . GLU   A 1 5   ? -41.089 7.861  28.253  1.00 81.82 ? 36  GLU   A OE2  1 
ATOM   10   N  N    . ALA   A 1 6   ? -38.000 11.971 26.369  1.00 65.40 ? 37  ALA   A N    1 
ATOM   11   C  CA   . ALA   A 1 6   ? -37.861 13.423 26.307  1.00 56.95 ? 37  ALA   A CA   1 
ATOM   12   C  C    . ALA   A 1 6   ? -38.630 14.128 27.420  1.00 55.76 ? 37  ALA   A C    1 
ATOM   13   O  O    . ALA   A 1 6   ? -39.782 13.793 27.711  1.00 57.00 ? 37  ALA   A O    1 
ATOM   14   C  CB   . ALA   A 1 6   ? -38.353 13.940 24.956  1.00 57.26 ? 37  ALA   A CB   1 
ATOM   15   N  N    . VAL   A 1 7   ? -37.989 15.125 28.034  1.00 50.51 ? 38  VAL   A N    1 
ATOM   16   C  CA   . VAL   A 1 7   ? -38.721 16.096 28.837  1.00 45.51 ? 38  VAL   A CA   1 
ATOM   17   C  C    . VAL   A 1 7   ? -39.718 16.817 27.943  1.00 49.37 ? 38  VAL   A C    1 
ATOM   18   O  O    . VAL   A 1 7   ? -39.338 17.425 26.934  1.00 50.44 ? 38  VAL   A O    1 
ATOM   19   C  CB   . VAL   A 1 7   ? -37.765 17.102 29.474  1.00 45.45 ? 38  VAL   A CB   1 
ATOM   20   C  CG1  . VAL   A 1 7   ? -38.523 17.995 30.455  1.00 47.37 ? 38  VAL   A CG1  1 
ATOM   21   C  CG2  . VAL   A 1 7   ? -36.590 16.402 30.118  1.00 51.18 ? 38  VAL   A CG2  1 
ATOM   22   N  N    . VAL   A 1 8   ? -40.991 16.780 28.313  1.00 46.04 ? 39  VAL   A N    1 
ATOM   23   C  CA   . VAL   A 1 8   ? -42.008 17.559 27.619  1.00 45.31 ? 39  VAL   A CA   1 
ATOM   24   C  C    . VAL   A 1 8   ? -42.115 18.916 28.299  1.00 47.00 ? 39  VAL   A C    1 
ATOM   25   O  O    . VAL   A 1 8   ? -42.405 18.998 29.495  1.00 47.49 ? 39  VAL   A O    1 
ATOM   26   C  CB   . VAL   A 1 8   ? -43.359 16.836 27.607  1.00 46.20 ? 39  VAL   A CB   1 
ATOM   27   C  CG1  . VAL   A 1 8   ? -44.386 17.660 26.832  1.00 43.87 ? 39  VAL   A CG1  1 
ATOM   28   C  CG2  . VAL   A 1 8   ? -43.197 15.468 26.981  1.00 51.02 ? 39  VAL   A CG2  1 
ATOM   29   N  N    . ILE   A 1 9   ? -41.870 19.981 27.539  1.00 46.01 ? 40  ILE   A N    1 
ATOM   30   C  CA   . ILE   A 1 9   ? -41.873 21.340 28.068  1.00 41.69 ? 40  ILE   A CA   1 
ATOM   31   C  C    . ILE   A 1 9   ? -43.297 21.872 27.982  1.00 40.06 ? 40  ILE   A C    1 
ATOM   32   O  O    . ILE   A 1 9   ? -43.887 21.924 26.902  1.00 43.48 ? 40  ILE   A O    1 
ATOM   33   C  CB   . ILE   A 1 9   ? -40.891 22.240 27.294  1.00 42.31 ? 40  ILE   A CB   1 
ATOM   34   C  CG1  . ILE   A 1 9   ? -39.452 21.744 27.442  1.00 41.45 ? 40  ILE   A CG1  1 
ATOM   35   C  CG2  . ILE   A 1 9   ? -40.975 23.679 27.748  1.00 39.66 ? 40  ILE   A CG2  1 
ATOM   36   C  CD1  . ILE   A 1 9   ? -38.488 22.357 26.397  1.00 40.84 ? 40  ILE   A CD1  1 
ATOM   37   N  N    . SER   A 1 10  ? -43.864 22.266 29.111  1.00 41.95 ? 41  SER   A N    1 
ATOM   38   C  CA   . SER   A 1 10  ? -45.220 22.804 29.090  1.00 41.86 ? 41  SER   A CA   1 
ATOM   39   C  C    . SER   A 1 10  ? -45.140 24.286 28.761  1.00 39.99 ? 41  SER   A C    1 
ATOM   40   O  O    . SER   A 1 10  ? -44.811 25.106 29.618  1.00 37.81 ? 41  SER   A O    1 
ATOM   41   C  CB   . SER   A 1 10  ? -45.928 22.581 30.420  1.00 44.36 ? 41  SER   A CB   1 
ATOM   42   O  OG   . SER   A 1 10  ? -47.242 23.101 30.342  1.00 44.74 ? 41  SER   A OG   1 
ATOM   43   N  N    . GLY   A 1 11  ? -45.433 24.639 27.507  1.00 40.50 ? 42  GLY   A N    1 
ATOM   44   C  CA   . GLY   A 1 11  ? -45.549 26.048 27.174  1.00 38.47 ? 42  GLY   A CA   1 
ATOM   45   C  C    . GLY   A 1 11  ? -46.659 26.712 27.959  1.00 35.07 ? 42  GLY   A C    1 
ATOM   46   O  O    . GLY   A 1 11  ? -46.541 27.870 28.370  1.00 34.50 ? 42  GLY   A O    1 
ATOM   47   N  N    . ARG   A 1 12  ? -47.749 25.979 28.188  1.00 36.31 ? 43  ARG   A N    1 
ATOM   48   C  CA   . ARG   A 1 12  ? -48.860 26.510 28.969  1.00 43.10 ? 43  ARG   A CA   1 
ATOM   49   C  C    . ARG   A 1 12  ? -48.392 26.934 30.358  1.00 39.74 ? 43  ARG   A C    1 
ATOM   50   O  O    . ARG   A 1 12  ? -48.660 28.056 30.806  1.00 40.12 ? 43  ARG   A O    1 
ATOM   51   C  CB   . ARG   A 1 12  ? -49.967 25.459 29.062  1.00 45.72 ? 43  ARG   A CB   1 
ATOM   52   C  CG   . ARG   A 1 12  ? -51.232 25.947 29.750  1.00 50.36 ? 43  ARG   A CG   1 
ATOM   53   C  CD   . ARG   A 1 12  ? -51.993 24.804 30.405  1.00 54.45 ? 43  ARG   A CD   1 
ATOM   54   N  NE   . ARG   A 1 12  ? -51.755 24.780 31.843  1.00 63.52 ? 43  ARG   A NE   1 
ATOM   55   C  CZ   . ARG   A 1 12  ? -50.927 23.954 32.473  1.00 61.33 ? 43  ARG   A CZ   1 
ATOM   56   N  NH1  . ARG   A 1 12  ? -50.637 24.118 33.758  1.00 48.18 ? 43  ARG   A NH1  1 
ATOM   57   N  NH2  . ARG   A 1 12  ? -50.381 22.936 31.803  1.00 57.63 ? 43  ARG   A NH2  1 
ATOM   58   N  N    . LYS   A 1 13  ? -47.646 26.063 31.031  1.00 41.02 ? 44  LYS   A N    1 
ATOM   59   C  CA   . LYS   A 1 13  ? -47.204 26.355 32.394  1.00 39.41 ? 44  LYS   A CA   1 
ATOM   60   C  C    . LYS   A 1 13  ? -46.200 27.509 32.426  1.00 38.57 ? 44  LYS   A C    1 
ATOM   61   O  O    . LYS   A 1 13  ? -46.304 28.399 33.271  1.00 35.61 ? 44  LYS   A O    1 
ATOM   62   C  CB   . LYS   A 1 13  ? -46.613 25.084 32.999  1.00 41.26 ? 44  LYS   A CB   1 
ATOM   63   C  CG   . LYS   A 1 13  ? -46.332 25.140 34.472  1.00 40.27 ? 44  LYS   A CG   1 
ATOM   64   C  CD   . LYS   A 1 13  ? -45.738 23.818 34.935  1.00 51.01 ? 44  LYS   A CD   1 
ATOM   65   C  CE   . LYS   A 1 13  ? -46.818 22.816 35.295  1.00 51.28 ? 44  LYS   A CE   1 
ATOM   66   N  NZ   . LYS   A 1 13  ? -47.287 23.076 36.668  1.00 43.07 ? 44  LYS   A NZ   1 
ATOM   67   N  N    . LEU   A 1 14  ? -45.248 27.540 31.480  1.00 38.88 ? 45  LEU   A N    1 
ATOM   68   C  CA   . LEU   A 1 14  ? -44.297 28.648 31.416  1.00 35.71 ? 45  LEU   A CA   1 
ATOM   69   C  C    . LEU   A 1 14  ? -45.009 29.963 31.162  1.00 35.18 ? 45  LEU   A C    1 
ATOM   70   O  O    . LEU   A 1 14  ? -44.705 30.983 31.795  1.00 33.05 ? 45  LEU   A O    1 
ATOM   71   C  CB   . LEU   A 1 14  ? -43.273 28.409 30.305  1.00 36.68 ? 45  LEU   A CB   1 
ATOM   72   C  CG   . LEU   A 1 14  ? -41.905 27.842 30.648  1.00 43.91 ? 45  LEU   A CG   1 
ATOM   73   C  CD1  . LEU   A 1 14  ? -41.098 27.711 29.354  1.00 43.60 ? 45  LEU   A CD1  1 
ATOM   74   C  CD2  . LEU   A 1 14  ? -41.184 28.741 31.647  1.00 46.18 ? 45  LEU   A CD2  1 
ATOM   75   N  N    . ALA   A 1 15  ? -45.939 29.961 30.202  1.00 35.23 ? 46  ALA   A N    1 
ATOM   76   C  CA   . ALA   A 1 15  ? -46.681 31.171 29.873  1.00 33.32 ? 46  ALA   A CA   1 
ATOM   77   C  C    . ALA   A 1 15  ? -47.437 31.691 31.086  1.00 35.42 ? 46  ALA   A C    1 
ATOM   78   O  O    . ALA   A 1 15  ? -47.466 32.900 31.340  1.00 33.14 ? 46  ALA   A O    1 
ATOM   79   C  CB   . ALA   A 1 15  ? -47.656 30.894 28.723  1.00 31.67 ? 46  ALA   A CB   1 
ATOM   80   N  N    . GLN   A 1 16  ? -48.075 30.788 31.834  1.00 35.46 ? 47  GLN   A N    1 
ATOM   81   C  CA   . GLN   A 1 16  ? -48.835 31.209 33.006  1.00 40.05 ? 47  GLN   A CA   1 
ATOM   82   C  C    . GLN   A 1 16  ? -47.921 31.837 34.057  1.00 31.15 ? 47  GLN   A C    1 
ATOM   83   O  O    . GLN   A 1 16  ? -48.272 32.857 34.662  1.00 34.52 ? 47  GLN   A O    1 
ATOM   84   C  CB   . GLN   A 1 16  ? -49.629 30.022 33.564  1.00 38.36 ? 47  GLN   A CB   1 
ATOM   85   C  CG   . GLN   A 1 16  ? -50.903 29.724 32.749  1.00 41.86 ? 47  GLN   A CG   1 
ATOM   86   C  CD   . GLN   A 1 16  ? -51.413 28.308 32.940  1.00 51.49 ? 47  GLN   A CD   1 
ATOM   87   O  OE1  . GLN   A 1 16  ? -50.650 27.403 33.294  1.00 53.41 ? 47  GLN   A OE1  1 
ATOM   88   N  NE2  . GLN   A 1 16  ? -52.711 28.106 32.717  1.00 50.28 ? 47  GLN   A NE2  1 
ATOM   89   N  N    . GLN   A 1 17  ? -46.719 31.286 34.243  1.00 37.15 ? 48  GLN   A N    1 
ATOM   90   C  CA   . GLN   A 1 17  ? -45.751 31.949 35.119  1.00 36.48 ? 48  GLN   A CA   1 
ATOM   91   C  C    . GLN   A 1 17  ? -45.432 33.353 34.617  1.00 37.10 ? 48  GLN   A C    1 
ATOM   92   O  O    . GLN   A 1 17  ? -45.487 34.328 35.376  1.00 32.56 ? 48  GLN   A O    1 
ATOM   93   C  CB   . GLN   A 1 17  ? -44.459 31.133 35.228  1.00 38.08 ? 48  GLN   A CB   1 
ATOM   94   C  CG   . GLN   A 1 17  ? -43.699 31.502 36.497  1.00 44.35 ? 48  GLN   A CG   1 
ATOM   95   C  CD   . GLN   A 1 17  ? -42.304 30.951 36.554  1.00 45.17 ? 48  GLN   A CD   1 
ATOM   96   O  OE1  . GLN   A 1 17  ? -41.928 30.068 35.777  1.00 44.73 ? 48  GLN   A OE1  1 
ATOM   97   N  NE2  . GLN   A 1 17  ? -41.513 31.474 37.488  1.00 50.45 ? 48  GLN   A NE2  1 
ATOM   98   N  N    . ILE   A 1 18  ? -45.128 33.479 33.316  1.00 36.00 ? 49  ILE   A N    1 
ATOM   99   C  CA   . ILE   A 1 18  ? -44.777 34.782 32.758  1.00 31.87 ? 49  ILE   A CA   1 
ATOM   100  C  C    . ILE   A 1 18  ? -45.916 35.770 32.944  1.00 28.51 ? 49  ILE   A C    1 
ATOM   101  O  O    . ILE   A 1 18  ? -45.694 36.940 33.273  1.00 34.94 ? 49  ILE   A O    1 
ATOM   102  C  CB   . ILE   A 1 18  ? -44.386 34.631 31.276  1.00 31.23 ? 49  ILE   A CB   1 
ATOM   103  C  CG1  . ILE   A 1 18  ? -43.027 33.946 31.190  1.00 32.95 ? 49  ILE   A CG1  1 
ATOM   104  C  CG2  . ILE   A 1 18  ? -44.355 35.992 30.597  1.00 33.36 ? 49  ILE   A CG2  1 
ATOM   105  C  CD1  . ILE   A 1 18  ? -42.728 33.339 29.807  1.00 38.96 ? 49  ILE   A CD1  1 
ATOM   106  N  N    . LYS   A 1 19  ? -47.154 35.314 32.763  1.00 28.71 ? 50  LYS   A N    1 
ATOM   107  C  CA   . LYS   A 1 19  ? -48.294 36.216 32.915  1.00 29.30 ? 50  LYS   A CA   1 
ATOM   108  C  C    . LYS   A 1 19  ? -48.396 36.718 34.348  1.00 34.77 ? 50  LYS   A C    1 
ATOM   109  O  O    . LYS   A 1 19  ? -48.758 37.880 34.592  1.00 34.18 ? 50  LYS   A O    1 
ATOM   110  C  CB   . LYS   A 1 19  ? -49.581 35.510 32.488  1.00 31.09 ? 50  LYS   A CB   1 
ATOM   111  C  CG   . LYS   A 1 19  ? -49.697 35.356 30.925  1.00 33.02 ? 50  LYS   A CG   1 
ATOM   112  C  CD   . LYS   A 1 19  ? -51.027 34.704 30.544  1.00 36.97 ? 50  LYS   A CD   1 
ATOM   113  C  CE   . LYS   A 1 19  ? -50.960 33.185 30.602  1.00 40.05 ? 50  LYS   A CE   1 
ATOM   114  N  NZ   . LYS   A 1 19  ? -52.331 32.569 30.515  1.00 43.31 ? 50  LYS   A NZ   1 
ATOM   115  N  N    . GLN   A 1 20  ? -48.060 35.863 35.314  1.00 33.87 ? 51  GLN   A N    1 
ATOM   116  C  CA   . GLN   A 1 20  ? -48.054 36.333 36.697  1.00 35.60 ? 51  GLN   A CA   1 
ATOM   117  C  C    . GLN   A 1 20  ? -47.005 37.420 36.887  1.00 32.72 ? 51  GLN   A C    1 
ATOM   118  O  O    . GLN   A 1 20  ? -47.274 38.446 37.522  1.00 38.05 ? 51  GLN   A O    1 
ATOM   119  C  CB   . GLN   A 1 20  ? -47.848 35.154 37.646  1.00 36.34 ? 51  GLN   A CB   1 
ATOM   120  C  CG   . GLN   A 1 20  ? -49.141 34.351 37.832  1.00 40.93 ? 51  GLN   A CG   1 
ATOM   121  C  CD   . GLN   A 1 20  ? -50.331 35.251 38.209  1.00 48.55 ? 51  GLN   A CD   1 
ATOM   122  O  OE1  . GLN   A 1 20  ? -50.352 35.847 39.299  1.00 41.69 ? 51  GLN   A OE1  1 
ATOM   123  N  NE2  . GLN   A 1 20  ? -51.314 35.367 37.297  1.00 44.35 ? 51  GLN   A NE2  1 
ATOM   124  N  N    . GLU   A 1 21  ? -45.830 37.250 36.277  1.00 34.29 ? 52  GLU   A N    1 
ATOM   125  C  CA   . GLU   A 1 21  ? -44.808 38.295 36.322  1.00 34.83 ? 52  GLU   A CA   1 
ATOM   126  C  C    . GLU   A 1 21  ? -45.309 39.597 35.711  1.00 38.21 ? 52  GLU   A C    1 
ATOM   127  O  O    . GLU   A 1 21  ? -45.039 40.680 36.243  1.00 37.97 ? 52  GLU   A O    1 
ATOM   128  C  CB   . GLU   A 1 21  ? -43.538 37.824 35.607  1.00 36.26 ? 52  GLU   A CB   1 
ATOM   129  C  CG   . GLU   A 1 21  ? -42.915 36.601 36.254  1.00 41.81 ? 52  GLU   A CG   1 
ATOM   130  C  CD   . GLU   A 1 21  ? -41.839 35.975 35.400  1.00 43.85 ? 52  GLU   A CD   1 
ATOM   131  O  OE1  . GLU   A 1 21  ? -41.507 36.559 34.353  1.00 44.02 ? 52  GLU   A OE1  1 
ATOM   132  O  OE2  . GLU   A 1 21  ? -41.344 34.888 35.767  1.00 47.13 ? 52  GLU   A OE2  1 
ATOM   133  N  N    . VAL   A 1 22  ? -46.033 39.518 34.586  1.00 34.50 ? 53  VAL   A N    1 
ATOM   134  C  CA   . VAL   A 1 22  ? -46.594 40.726 33.988  1.00 30.10 ? 53  VAL   A CA   1 
ATOM   135  C  C    . VAL   A 1 22  ? -47.655 41.340 34.893  1.00 31.45 ? 53  VAL   A C    1 
ATOM   136  O  O    . VAL   A 1 22  ? -47.721 42.565 35.049  1.00 31.02 ? 53  VAL   A O    1 
ATOM   137  C  CB   . VAL   A 1 22  ? -47.166 40.417 32.586  1.00 34.20 ? 53  VAL   A CB   1 
ATOM   138  C  CG1  . VAL   A 1 22  ? -47.781 41.658 31.985  1.00 30.01 ? 53  VAL   A CG1  1 
ATOM   139  C  CG2  . VAL   A 1 22  ? -46.071 39.886 31.689  1.00 30.90 ? 53  VAL   A CG2  1 
ATOM   140  N  N    . ARG   A 1 23  ? -48.537 40.511 35.452  1.00 27.27 ? 54  ARG   A N    1 
ATOM   141  C  CA   . ARG   A 1 23  ? -49.569 41.034 36.345  1.00 36.69 ? 54  ARG   A CA   1 
ATOM   142  C  C    . ARG   A 1 23  ? -48.950 41.883 37.455  1.00 36.65 ? 54  ARG   A C    1 
ATOM   143  O  O    . ARG   A 1 23  ? -49.409 42.998 37.729  1.00 36.71 ? 54  ARG   A O    1 
ATOM   144  C  CB   . ARG   A 1 23  ? -50.382 39.889 36.950  1.00 35.65 ? 54  ARG   A CB   1 
ATOM   145  C  CG   . ARG   A 1 23  ? -51.555 40.366 37.786  1.00 39.98 ? 54  ARG   A CG   1 
ATOM   146  C  CD   . ARG   A 1 23  ? -52.347 39.201 38.332  1.00 46.62 ? 54  ARG   A CD   1 
ATOM   147  N  NE   . ARG   A 1 23  ? -53.266 39.640 39.376  1.00 61.84 ? 54  ARG   A NE   1 
ATOM   148  C  CZ   . ARG   A 1 23  ? -53.775 38.842 40.306  1.00 66.39 ? 54  ARG   A CZ   1 
ATOM   149  N  NH1  . ARG   A 1 23  ? -53.504 37.545 40.330  1.00 62.86 ? 54  ARG   A NH1  1 
ATOM   150  N  NH2  . ARG   A 1 23  ? -54.564 39.359 41.244  1.00 72.58 ? 54  ARG   A NH2  1 
ATOM   151  N  N    . GLN   A 1 24  ? -47.866 41.386 38.061  1.00 37.21 ? 55  GLN   A N    1 
ATOM   152  C  CA   . GLN   A 1 24  ? -47.186 42.133 39.124  1.00 40.88 ? 55  GLN   A CA   1 
ATOM   153  C  C    . GLN   A 1 24  ? -46.619 43.439 38.603  1.00 41.95 ? 55  GLN   A C    1 
ATOM   154  O  O    . GLN   A 1 24  ? -46.727 44.477 39.264  1.00 41.24 ? 55  GLN   A O    1 
ATOM   155  C  CB   . GLN   A 1 24  ? -46.068 41.292 39.736  1.00 42.36 ? 55  GLN   A CB   1 
ATOM   156  C  CG   . GLN   A 1 24  ? -46.556 40.301 40.754  1.00 46.33 ? 55  GLN   A CG   1 
ATOM   157  C  CD   . GLN   A 1 24  ? -45.611 39.122 40.915  1.00 52.11 ? 55  GLN   A CD   1 
ATOM   158  O  OE1  . GLN   A 1 24  ? -44.516 39.096 40.331  1.00 45.05 ? 55  GLN   A OE1  1 
ATOM   159  N  NE2  . GLN   A 1 24  ? -46.035 38.129 41.700  1.00 51.11 ? 55  GLN   A NE2  1 
ATOM   160  N  N    . GLU   A 1 25  ? -46.017 43.410 37.415  1.00 37.52 ? 56  GLU   A N    1 
ATOM   161  C  CA   . GLU   A 1 25  ? -45.461 44.629 36.842  1.00 39.41 ? 56  GLU   A CA   1 
ATOM   162  C  C    . GLU   A 1 25  ? -46.558 45.637 36.530  1.00 41.24 ? 56  GLU   A C    1 
ATOM   163  O  O    . GLU   A 1 25  ? -46.397 46.841 36.762  1.00 40.39 ? 56  GLU   A O    1 
ATOM   164  C  CB   . GLU   A 1 25  ? -44.669 44.279 35.581  1.00 39.87 ? 56  GLU   A CB   1 
ATOM   165  C  CG   . GLU   A 1 25  ? -43.989 45.455 34.937  1.00 43.45 ? 56  GLU   A CG   1 
ATOM   166  C  CD   . GLU   A 1 25  ? -43.114 45.051 33.772  1.00 48.39 ? 56  GLU   A CD   1 
ATOM   167  O  OE1  . GLU   A 1 25  ? -43.119 43.857 33.394  1.00 49.16 ? 56  GLU   A OE1  1 
ATOM   168  O  OE2  . GLU   A 1 25  ? -42.424 45.936 33.226  1.00 52.62 ? 56  GLU   A OE2  1 
ATOM   169  N  N    . VAL   A 1 26  ? -47.676 45.163 35.979  1.00 40.32 ? 57  VAL   A N    1 
ATOM   170  C  CA   . VAL   A 1 26  ? -48.795 46.051 35.687  1.00 35.82 ? 57  VAL   A CA   1 
ATOM   171  C  C    . VAL   A 1 26  ? -49.375 46.639 36.975  1.00 36.39 ? 57  VAL   A C    1 
ATOM   172  O  O    . VAL   A 1 26  ? -49.664 47.836 37.044  1.00 38.37 ? 57  VAL   A O    1 
ATOM   173  C  CB   . VAL   A 1 26  ? -49.861 45.294 34.873  1.00 37.13 ? 57  VAL   A CB   1 
ATOM   174  C  CG1  . VAL   A 1 26  ? -51.165 46.086 34.850  1.00 34.59 ? 57  VAL   A CG1  1 
ATOM   175  C  CG2  . VAL   A 1 26  ? -49.315 44.993 33.431  1.00 29.66 ? 57  VAL   A CG2  1 
ATOM   176  N  N    . GLU   A 1 27  ? -49.559 45.812 38.007  1.00 40.06 ? 58  GLU   A N    1 
ATOM   177  C  CA   . GLU   A 1 27  ? -50.171 46.306 39.249  1.00 45.61 ? 58  GLU   A CA   1 
ATOM   178  C  C    . GLU   A 1 27  ? -49.310 47.379 39.912  1.00 45.47 ? 58  GLU   A C    1 
ATOM   179  O  O    . GLU   A 1 27  ? -49.837 48.350 40.474  1.00 47.99 ? 58  GLU   A O    1 
ATOM   180  C  CB   . GLU   A 1 27  ? -50.437 45.159 40.231  1.00 42.40 ? 58  GLU   A CB   1 
ATOM   181  C  CG   . GLU   A 1 27  ? -51.526 44.143 39.803  1.00 45.32 ? 58  GLU   A CG   1 
ATOM   182  C  CD   . GLU   A 1 27  ? -52.583 44.712 38.829  1.00 57.31 ? 58  GLU   A CD   1 
ATOM   183  O  OE1  . GLU   A 1 27  ? -53.375 45.594 39.239  1.00 56.86 ? 58  GLU   A OE1  1 
ATOM   184  O  OE2  . GLU   A 1 27  ? -52.612 44.267 37.642  1.00 50.90 ? 58  GLU   A OE2  1 
ATOM   185  N  N    . GLU   A 1 28  ? -47.984 47.227 39.853  1.00 46.57 ? 59  GLU   A N    1 
ATOM   186  C  CA   . GLU   A 1 28  ? -47.101 48.237 40.434  1.00 48.61 ? 59  GLU   A CA   1 
ATOM   187  C  C    . GLU   A 1 28  ? -47.031 49.486 39.573  1.00 48.82 ? 59  GLU   A C    1 
ATOM   188  O  O    . GLU   A 1 28  ? -46.861 50.591 40.106  1.00 48.51 ? 59  GLU   A O    1 
ATOM   189  C  CB   . GLU   A 1 28  ? -45.710 47.646 40.658  1.00 49.33 ? 59  GLU   A CB   1 
ATOM   190  C  CG   . GLU   A 1 28  ? -45.748 46.515 41.705  1.00 54.82 ? 59  GLU   A CG   1 
ATOM   191  C  CD   . GLU   A 1 28  ? -46.423 46.919 43.022  1.00 53.60 ? 59  GLU   A CD   1 
ATOM   192  O  OE1  . GLU   A 1 28  ? -45.863 47.770 43.743  1.00 54.39 ? 59  GLU   A OE1  1 
ATOM   193  O  OE2  . GLU   A 1 28  ? -47.517 46.390 43.334  1.00 59.72 ? 59  GLU   A OE2  1 
ATOM   194  N  N    . TRP   A 1 29  ? -47.161 49.330 38.251  1.00 43.75 ? 60  TRP   A N    1 
ATOM   195  C  CA   . TRP   A 1 29  ? -47.264 50.480 37.355  1.00 44.01 ? 60  TRP   A CA   1 
ATOM   196  C  C    . TRP   A 1 29  ? -48.508 51.307 37.665  1.00 41.84 ? 60  TRP   A C    1 
ATOM   197  O  O    . TRP   A 1 29  ? -48.466 52.543 37.647  1.00 42.87 ? 60  TRP   A O    1 
ATOM   198  C  CB   . TRP   A 1 29  ? -47.279 49.985 35.894  1.00 42.07 ? 60  TRP   A CB   1 
ATOM   199  C  CG   . TRP   A 1 29  ? -47.314 51.042 34.814  1.00 42.93 ? 60  TRP   A CG   1 
ATOM   200  C  CD1  . TRP   A 1 29  ? -48.341 51.285 33.927  1.00 45.58 ? 60  TRP   A CD1  1 
ATOM   201  C  CD2  . TRP   A 1 29  ? -46.266 51.957 34.460  1.00 44.62 ? 60  TRP   A CD2  1 
ATOM   202  N  NE1  . TRP   A 1 29  ? -47.998 52.305 33.072  1.00 44.46 ? 60  TRP   A NE1  1 
ATOM   203  C  CE2  . TRP   A 1 29  ? -46.735 52.740 33.386  1.00 44.89 ? 60  TRP   A CE2  1 
ATOM   204  C  CE3  . TRP   A 1 29  ? -44.984 52.203 34.961  1.00 50.10 ? 60  TRP   A CE3  1 
ATOM   205  C  CZ2  . TRP   A 1 29  ? -45.966 53.741 32.803  1.00 50.98 ? 60  TRP   A CZ2  1 
ATOM   206  C  CZ3  . TRP   A 1 29  ? -44.226 53.200 34.381  1.00 48.14 ? 60  TRP   A CZ3  1 
ATOM   207  C  CH2  . TRP   A 1 29  ? -44.716 53.953 33.315  1.00 47.44 ? 60  TRP   A CH2  1 
ATOM   208  N  N    . VAL   A 1 30  ? -49.633 50.637 37.914  1.00 39.48 ? 61  VAL   A N    1 
ATOM   209  C  CA   . VAL   A 1 30  ? -50.865 51.339 38.249  1.00 41.54 ? 61  VAL   A CA   1 
ATOM   210  C  C    . VAL   A 1 30  ? -50.771 51.934 39.651  1.00 46.39 ? 61  VAL   A C    1 
ATOM   211  O  O    . VAL   A 1 30  ? -51.065 53.119 39.868  1.00 43.71 ? 61  VAL   A O    1 
ATOM   212  C  CB   . VAL   A 1 30  ? -52.064 50.385 38.116  1.00 43.30 ? 61  VAL   A CB   1 
ATOM   213  C  CG1  . VAL   A 1 30  ? -53.312 51.018 38.717  1.00 39.77 ? 61  VAL   A CG1  1 
ATOM   214  C  CG2  . VAL   A 1 30  ? -52.290 50.007 36.619  1.00 38.69 ? 61  VAL   A CG2  1 
ATOM   215  N  N    . ALA   A 1 31  ? -50.315 51.131 40.614  1.00 40.16 ? 62  ALA   A N    1 
ATOM   216  C  CA   . ALA   A 1 31  ? -50.166 51.625 41.984  1.00 47.38 ? 62  ALA   A CA   1 
ATOM   217  C  C    . ALA   A 1 31  ? -49.209 52.810 42.072  1.00 46.48 ? 62  ALA   A C    1 
ATOM   218  O  O    . ALA   A 1 31  ? -49.298 53.586 43.027  1.00 56.01 ? 62  ALA   A O    1 
ATOM   219  C  CB   . ALA   A 1 31  ? -49.701 50.492 42.901  1.00 41.20 ? 62  ALA   A CB   1 
ATOM   220  N  N    . SER   A 1 32  ? -48.317 52.987 41.091  1.00 48.69 ? 63  SER   A N    1 
ATOM   221  C  CA   . SER   A 1 32  ? -47.437 54.150 41.045  1.00 46.52 ? 63  SER   A CA   1 
ATOM   222  C  C    . SER   A 1 32  ? -48.114 55.382 40.472  1.00 48.17 ? 63  SER   A C    1 
ATOM   223  O  O    . SER   A 1 32  ? -47.446 56.411 40.310  1.00 49.41 ? 63  SER   A O    1 
ATOM   224  C  CB   . SER   A 1 32  ? -46.183 53.852 40.224  1.00 49.21 ? 63  SER   A CB   1 
ATOM   225  O  OG   . SER   A 1 32  ? -45.359 52.905 40.873  1.00 48.16 ? 63  SER   A OG   1 
ATOM   226  N  N    . GLY   A 1 33  ? -49.406 55.303 40.157  1.00 46.51 ? 64  GLY   A N    1 
ATOM   227  C  CA   . GLY   A 1 33  ? -50.139 56.434 39.634  1.00 44.98 ? 64  GLY   A CA   1 
ATOM   228  C  C    . GLY   A 1 33  ? -50.242 56.515 38.124  1.00 48.37 ? 64  GLY   A C    1 
ATOM   229  O  O    . GLY   A 1 33  ? -50.625 57.571 37.606  1.00 49.54 ? 64  GLY   A O    1 
ATOM   230  N  N    . ASN   A 1 34  ? -49.906 55.451 37.401  1.00 45.67 ? 65  ASN   A N    1 
ATOM   231  C  CA   . ASN   A 1 34  ? -49.968 55.449 35.945  1.00 44.59 ? 65  ASN   A CA   1 
ATOM   232  C  C    . ASN   A 1 34  ? -51.274 54.821 35.475  1.00 44.89 ? 65  ASN   A C    1 
ATOM   233  O  O    . ASN   A 1 34  ? -51.847 53.973 36.158  1.00 43.94 ? 65  ASN   A O    1 
ATOM   234  C  CB   . ASN   A 1 34  ? -48.788 54.681 35.351  1.00 44.36 ? 65  ASN   A CB   1 
ATOM   235  C  CG   . ASN   A 1 34  ? -47.451 55.280 35.729  1.00 45.77 ? 65  ASN   A CG   1 
ATOM   236  O  OD1  . ASN   A 1 34  ? -47.000 56.245 35.119  1.00 47.32 ? 65  ASN   A OD1  1 
ATOM   237  N  ND2  . ASN   A 1 34  ? -46.802 54.696 36.728  1.00 46.40 ? 65  ASN   A ND2  1 
ATOM   238  N  N    . LYS   A 1 35  ? -51.732 55.223 34.287  1.00 48.44 ? 66  LYS   A N    1 
ATOM   239  C  CA   . LYS   A 1 35  ? -52.970 54.660 33.758  1.00 43.14 ? 66  LYS   A CA   1 
ATOM   240  C  C    . LYS   A 1 35  ? -52.796 53.169 33.492  1.00 40.53 ? 66  LYS   A C    1 
ATOM   241  O  O    . LYS   A 1 35  ? -51.707 52.697 33.152  1.00 43.21 ? 66  LYS   A O    1 
ATOM   242  C  CB   . LYS   A 1 35  ? -53.396 55.380 32.478  1.00 45.44 ? 66  LYS   A CB   1 
ATOM   243  C  CG   . LYS   A 1 35  ? -52.574 55.019 31.271  1.00 51.50 ? 66  LYS   A CG   1 
ATOM   244  C  CD   . LYS   A 1 35  ? -53.159 55.594 29.983  1.00 53.02 ? 66  LYS   A CD   1 
ATOM   245  C  CE   . LYS   A 1 35  ? -54.248 54.707 29.416  1.00 49.88 ? 66  LYS   A CE   1 
ATOM   246  N  NZ   . LYS   A 1 35  ? -53.753 53.345 29.089  1.00 44.20 ? 66  LYS   A NZ   1 
ATOM   247  N  N    . ARG   A 1 36  ? -53.870 52.417 33.695  1.00 35.55 ? 67  ARG   A N    1 
ATOM   248  C  CA   . ARG   A 1 36  ? -53.813 50.987 33.434  1.00 41.22 ? 67  ARG   A CA   1 
ATOM   249  C  C    . ARG   A 1 36  ? -53.592 50.767 31.934  1.00 39.68 ? 67  ARG   A C    1 
ATOM   250  O  O    . ARG   A 1 36  ? -54.140 51.516 31.117  1.00 41.37 ? 67  ARG   A O    1 
ATOM   251  C  CB   . ARG   A 1 36  ? -55.105 50.309 33.904  1.00 37.13 ? 67  ARG   A CB   1 
ATOM   252  C  CG   . ARG   A 1 36  ? -55.148 48.803 33.694  1.00 42.29 ? 67  ARG   A CG   1 
ATOM   253  C  CD   . ARG   A 1 36  ? -56.258 48.143 34.512  1.00 41.66 ? 67  ARG   A CD   1 
ATOM   254  N  NE   . ARG   A 1 36  ? -56.133 48.373 35.949  1.00 42.15 ? 67  ARG   A NE   1 
ATOM   255  C  CZ   . ARG   A 1 36  ? -55.546 47.538 36.800  1.00 45.84 ? 67  ARG   A CZ   1 
ATOM   256  N  NH1  . ARG   A 1 36  ? -54.954 46.428 36.389  1.00 39.57 ? 67  ARG   A NH1  1 
ATOM   257  N  NH2  . ARG   A 1 36  ? -55.553 47.823 38.100  1.00 44.46 ? 67  ARG   A NH2  1 
ATOM   258  N  N    . PRO   A 1 37  ? -52.751 49.804 31.541  1.00 39.10 ? 68  PRO   A N    1 
ATOM   259  C  CA   . PRO   A 1 37  ? -52.497 49.591 30.106  1.00 35.70 ? 68  PRO   A CA   1 
ATOM   260  C  C    . PRO   A 1 37  ? -53.756 49.123 29.386  1.00 40.71 ? 68  PRO   A C    1 
ATOM   261  O  O    . PRO   A 1 37  ? -54.642 48.495 29.977  1.00 37.94 ? 68  PRO   A O    1 
ATOM   262  C  CB   . PRO   A 1 37  ? -51.406 48.513 30.084  1.00 36.48 ? 68  PRO   A CB   1 
ATOM   263  C  CG   . PRO   A 1 37  ? -50.733 48.612 31.483  1.00 37.67 ? 68  PRO   A CG   1 
ATOM   264  C  CD   . PRO   A 1 37  ? -51.878 48.970 32.391  1.00 39.19 ? 68  PRO   A CD   1 
ATOM   265  N  N    . HIS   A 1 38  ? -53.834 49.462 28.095  1.00 36.19 ? 69  HIS   A N    1 
ATOM   266  C  CA   . HIS   A 1 38  ? -54.951 49.060 27.250  1.00 37.36 ? 69  HIS   A CA   1 
ATOM   267  C  C    . HIS   A 1 38  ? -54.412 48.550 25.918  1.00 33.67 ? 69  HIS   A C    1 
ATOM   268  O  O    . HIS   A 1 38  ? -53.629 49.237 25.258  1.00 36.95 ? 69  HIS   A O    1 
ATOM   269  C  CB   . HIS   A 1 38  ? -55.923 50.224 27.017  1.00 36.99 ? 69  HIS   A CB   1 
ATOM   270  C  CG   . HIS   A 1 38  ? -56.993 49.917 26.012  1.00 41.09 ? 69  HIS   A CG   1 
ATOM   271  N  ND1  . HIS   A 1 38  ? -58.275 49.558 26.373  1.00 39.17 ? 69  HIS   A ND1  1 
ATOM   272  C  CD2  . HIS   A 1 38  ? -56.963 49.894 24.655  1.00 40.11 ? 69  HIS   A CD2  1 
ATOM   273  C  CE1  . HIS   A 1 38  ? -58.994 49.344 25.282  1.00 43.24 ? 69  HIS   A CE1  1 
ATOM   274  N  NE2  . HIS   A 1 38  ? -58.220 49.536 24.226  1.00 40.00 ? 69  HIS   A NE2  1 
ATOM   275  N  N    . LEU   A 1 39  ? -54.840 47.353 25.533  1.00 34.19 ? 70  LEU   A N    1 
ATOM   276  C  CA   . LEU   A 1 39  ? -54.489 46.732 24.259  1.00 34.03 ? 70  LEU   A CA   1 
ATOM   277  C  C    . LEU   A 1 39  ? -55.691 46.728 23.328  1.00 33.31 ? 70  LEU   A C    1 
ATOM   278  O  O    . LEU   A 1 39  ? -56.760 46.229 23.691  1.00 33.99 ? 70  LEU   A O    1 
ATOM   279  C  CB   . LEU   A 1 39  ? -54.025 45.298 24.489  1.00 32.95 ? 70  LEU   A CB   1 
ATOM   280  C  CG   . LEU   A 1 39  ? -53.809 44.394 23.286  1.00 33.53 ? 70  LEU   A CG   1 
ATOM   281  C  CD1  . LEU   A 1 39  ? -52.472 44.700 22.640  1.00 34.15 ? 70  LEU   A CD1  1 
ATOM   282  C  CD2  . LEU   A 1 39  ? -53.878 42.951 23.738  1.00 29.36 ? 70  LEU   A CD2  1 
ATOM   283  N  N    . SER   A 1 40  ? -55.514 47.243 22.118  1.00 36.45 ? 71  SER   A N    1 
ATOM   284  C  CA   . SER   A 1 40  ? -56.536 47.120 21.082  1.00 35.90 ? 71  SER   A CA   1 
ATOM   285  C  C    . SER   A 1 40  ? -56.088 46.113 20.037  1.00 35.69 ? 71  SER   A C    1 
ATOM   286  O  O    . SER   A 1 40  ? -54.966 46.212 19.524  1.00 31.93 ? 71  SER   A O    1 
ATOM   287  C  CB   . SER   A 1 40  ? -56.817 48.465 20.421  1.00 38.33 ? 71  SER   A CB   1 
ATOM   288  O  OG   . SER   A 1 40  ? -57.461 49.319 21.336  1.00 40.21 ? 71  SER   A OG   1 
ATOM   289  N  N    . VAL   A 1 41  ? -56.974 45.165 19.714  1.00 33.12 ? 72  VAL   A N    1 
ATOM   290  C  CA   . VAL   A 1 41  ? -56.754 44.161 18.677  1.00 32.97 ? 72  VAL   A CA   1 
ATOM   291  C  C    . VAL   A 1 41  ? -57.799 44.349 17.579  1.00 37.25 ? 72  VAL   A C    1 
ATOM   292  O  O    . VAL   A 1 41  ? -59.008 44.368 17.856  1.00 33.76 ? 72  VAL   A O    1 
ATOM   293  C  CB   . VAL   A 1 41  ? -56.831 42.729 19.236  1.00 29.52 ? 72  VAL   A CB   1 
ATOM   294  C  CG1  . VAL   A 1 41  ? -56.552 41.699 18.124  1.00 28.93 ? 72  VAL   A CG1  1 
ATOM   295  C  CG2  . VAL   A 1 41  ? -55.872 42.557 20.424  1.00 33.10 ? 72  VAL   A CG2  1 
ATOM   296  N  N    . ILE   A 1 42  ? -57.339 44.472 16.338  1.00 33.77 ? 73  ILE   A N    1 
ATOM   297  C  CA   . ILE   A 1 42  ? -58.227 44.568 15.185  1.00 29.67 ? 73  ILE   A CA   1 
ATOM   298  C  C    . ILE   A 1 42  ? -58.278 43.198 14.534  1.00 30.26 ? 73  ILE   A C    1 
ATOM   299  O  O    . ILE   A 1 42  ? -57.239 42.600 14.228  1.00 33.11 ? 73  ILE   A O    1 
ATOM   300  C  CB   . ILE   A 1 42  ? -57.760 45.657 14.213  1.00 32.02 ? 73  ILE   A CB   1 
ATOM   301  C  CG1  . ILE   A 1 42  ? -57.796 47.010 14.933  1.00 30.18 ? 73  ILE   A CG1  1 
ATOM   302  C  CG2  . ILE   A 1 42  ? -58.642 45.672 12.936  1.00 34.16 ? 73  ILE   A CG2  1 
ATOM   303  C  CD1  . ILE   A 1 42  ? -57.197 48.152 14.130  1.00 37.06 ? 73  ILE   A CD1  1 
ATOM   304  N  N    . LEU   A 1 43  ? -59.479 42.663 14.379  1.00 31.56 ? 74  LEU   A N    1 
ATOM   305  C  CA   . LEU   A 1 43  ? -59.674 41.357 13.759  1.00 30.44 ? 74  LEU   A CA   1 
ATOM   306  C  C    . LEU   A 1 43  ? -60.525 41.552 12.504  1.00 34.11 ? 74  LEU   A C    1 
ATOM   307  O  O    . LEU   A 1 43  ? -61.614 42.127 12.569  1.00 37.02 ? 74  LEU   A O    1 
ATOM   308  C  CB   . LEU   A 1 43  ? -60.332 40.409 14.767  1.00 37.14 ? 74  LEU   A CB   1 
ATOM   309  C  CG   . LEU   A 1 43  ? -60.644 38.950 14.469  1.00 40.53 ? 74  LEU   A CG   1 
ATOM   310  C  CD1  . LEU   A 1 43  ? -59.409 38.148 14.023  1.00 37.26 ? 74  LEU   A CD1  1 
ATOM   311  C  CD2  . LEU   A 1 43  ? -61.263 38.365 15.741  1.00 37.29 ? 74  LEU   A CD2  1 
ATOM   312  N  N    . VAL   A 1 44  ? -60.023 41.102 11.360  1.00 31.65 ? 75  VAL   A N    1 
ATOM   313  C  CA   . VAL   A 1 44  ? -60.709 41.284 10.081  1.00 33.59 ? 75  VAL   A CA   1 
ATOM   314  C  C    . VAL   A 1 44  ? -61.150 39.918 9.570   1.00 34.77 ? 75  VAL   A C    1 
ATOM   315  O  O    . VAL   A 1 44  ? -60.327 39.002 9.448   1.00 36.15 ? 75  VAL   A O    1 
ATOM   316  C  CB   . VAL   A 1 44  ? -59.802 41.994 9.057   1.00 31.44 ? 75  VAL   A CB   1 
ATOM   317  C  CG1  . VAL   A 1 44  ? -60.505 42.104 7.684   1.00 34.36 ? 75  VAL   A CG1  1 
ATOM   318  C  CG2  . VAL   A 1 44  ? -59.412 43.382 9.552   1.00 29.65 ? 75  VAL   A CG2  1 
ATOM   319  N  N    . GLY   A 1 45  ? -62.441 39.780 9.262   1.00 36.61 ? 76  GLY   A N    1 
ATOM   320  C  CA   . GLY   A 1 45  ? -62.922 38.550 8.655   1.00 35.84 ? 76  GLY   A CA   1 
ATOM   321  C  C    . GLY   A 1 45  ? -63.265 37.462 9.659   1.00 40.68 ? 76  GLY   A C    1 
ATOM   322  O  O    . GLY   A 1 45  ? -63.441 37.704 10.859  1.00 41.86 ? 76  GLY   A O    1 
ATOM   323  N  N    . GLU   A 1 46  ? -63.329 36.227 9.158   1.00 40.68 ? 77  GLU   A N    1 
ATOM   324  C  CA   . GLU   A 1 46  ? -63.869 35.126 9.953   1.00 46.61 ? 77  GLU   A CA   1 
ATOM   325  C  C    . GLU   A 1 46  ? -62.930 33.926 10.006  1.00 44.41 ? 77  GLU   A C    1 
ATOM   326  O  O    . GLU   A 1 46  ? -63.390 32.779 10.084  1.00 45.45 ? 77  GLU   A O    1 
ATOM   327  C  CB   . GLU   A 1 46  ? -65.235 34.694 9.412   1.00 49.18 ? 77  GLU   A CB   1 
ATOM   328  C  CG   . GLU   A 1 46  ? -66.265 35.815 9.391   1.00 49.15 ? 77  GLU   A CG   1 
ATOM   329  C  CD   . GLU   A 1 46  ? -67.622 35.368 8.880   1.00 48.93 ? 77  GLU   A CD   1 
ATOM   330  O  OE1  . GLU   A 1 46  ? -67.771 34.185 8.510   1.00 46.97 ? 77  GLU   A OE1  1 
ATOM   331  O  OE2  . GLU   A 1 46  ? -68.545 36.207 8.863   1.00 50.15 ? 77  GLU   A OE2  1 
ATOM   332  N  N    . ASN   A 1 47  ? -61.625 34.149 9.954   1.00 39.96 ? 78  ASN   A N    1 
ATOM   333  C  CA   . ASN   A 1 47  ? -60.713 33.021 10.072  1.00 43.09 ? 78  ASN   A CA   1 
ATOM   334  C  C    . ASN   A 1 47  ? -60.886 32.426 11.470  1.00 43.41 ? 78  ASN   A C    1 
ATOM   335  O  O    . ASN   A 1 47  ? -60.677 33.138 12.469  1.00 41.74 ? 78  ASN   A O    1 
ATOM   336  C  CB   . ASN   A 1 47  ? -59.280 33.489 9.820   1.00 41.65 ? 78  ASN   A CB   1 
ATOM   337  C  CG   . ASN   A 1 47  ? -58.262 32.358 9.850   1.00 46.61 ? 78  ASN   A CG   1 
ATOM   338  O  OD1  . ASN   A 1 47  ? -58.288 31.485 10.728  1.00 45.73 ? 78  ASN   A OD1  1 
ATOM   339  N  ND2  . ASN   A 1 47  ? -57.324 32.395 8.902   1.00 38.89 ? 78  ASN   A ND2  1 
ATOM   340  N  N    . PRO   A 1 48  ? -61.322 31.166 11.595  1.00 45.53 ? 79  PRO   A N    1 
ATOM   341  C  CA   . PRO   A 1 48  ? -61.595 30.638 12.945  1.00 44.98 ? 79  PRO   A CA   1 
ATOM   342  C  C    . PRO   A 1 48  ? -60.357 30.553 13.821  1.00 42.86 ? 79  PRO   A C    1 
ATOM   343  O  O    . PRO   A 1 48  ? -60.438 30.815 15.031  1.00 39.16 ? 79  PRO   A O    1 
ATOM   344  C  CB   . PRO   A 1 48  ? -62.202 29.255 12.667  1.00 46.11 ? 79  PRO   A CB   1 
ATOM   345  C  CG   . PRO   A 1 48  ? -61.763 28.914 11.279  1.00 49.28 ? 79  PRO   A CG   1 
ATOM   346  C  CD   . PRO   A 1 48  ? -61.714 30.211 10.544  1.00 44.57 ? 79  PRO   A CD   1 
ATOM   347  N  N    . ALA   A 1 49  ? -59.212 30.188 13.236  1.00 43.57 ? 80  ALA   A N    1 
ATOM   348  C  CA   . ALA   A 1 49  ? -57.967 30.189 13.989  1.00 41.03 ? 80  ALA   A CA   1 
ATOM   349  C  C    . ALA   A 1 49  ? -57.656 31.580 14.521  1.00 42.69 ? 80  ALA   A C    1 
ATOM   350  O  O    . ALA   A 1 49  ? -57.300 31.732 15.701  1.00 39.89 ? 80  ALA   A O    1 
ATOM   351  C  CB   . ALA   A 1 49  ? -56.818 29.665 13.123  1.00 38.69 ? 80  ALA   A CB   1 
ATOM   352  N  N    . SER   A 1 50  ? -57.820 32.614 13.680  1.00 36.31 ? 81  SER   A N    1 
ATOM   353  C  CA   . SER   A 1 50  ? -57.577 33.982 14.129  1.00 38.15 ? 81  SER   A CA   1 
ATOM   354  C  C    . SER   A 1 50  ? -58.511 34.368 15.273  1.00 40.76 ? 81  SER   A C    1 
ATOM   355  O  O    . SER   A 1 50  ? -58.095 35.026 16.243  1.00 33.44 ? 81  SER   A O    1 
ATOM   356  C  CB   . SER   A 1 50  ? -57.733 34.959 12.965  1.00 36.42 ? 81  SER   A CB   1 
ATOM   357  O  OG   . SER   A 1 50  ? -56.805 34.659 11.932  1.00 35.75 ? 81  SER   A OG   1 
ATOM   358  N  N    . HIS   A 1 51  ? -59.784 33.994 15.169  1.00 35.58 ? 82  HIS   A N    1 
ATOM   359  C  CA   . HIS   A 1 51  ? -60.718 34.350 16.231  1.00 39.79 ? 82  HIS   A CA   1 
ATOM   360  C  C    . HIS   A 1 51  ? -60.340 33.666 17.539  1.00 37.82 ? 82  HIS   A C    1 
ATOM   361  O  O    . HIS   A 1 51  ? -60.364 34.289 18.603  1.00 36.40 ? 82  HIS   A O    1 
ATOM   362  C  CB   . HIS   A 1 51  ? -62.142 34.010 15.804  1.00 36.79 ? 82  HIS   A CB   1 
ATOM   363  C  CG   . HIS   A 1 51  ? -62.758 35.058 14.934  1.00 42.45 ? 82  HIS   A CG   1 
ATOM   364  N  ND1  . HIS   A 1 51  ? -63.714 35.938 15.395  1.00 40.99 ? 82  HIS   A ND1  1 
ATOM   365  C  CD2  . HIS   A 1 51  ? -62.524 35.398 13.642  1.00 37.84 ? 82  HIS   A CD2  1 
ATOM   366  C  CE1  . HIS   A 1 51  ? -64.062 36.758 14.417  1.00 43.19 ? 82  HIS   A CE1  1 
ATOM   367  N  NE2  . HIS   A 1 51  ? -63.349 36.458 13.347  1.00 37.10 ? 82  HIS   A NE2  1 
ATOM   368  N  N    . SER   A 1 52  ? -59.937 32.397 17.469  1.00 37.73 ? 83  SER   A N    1 
ATOM   369  C  CA   . SER   A 1 52  ? -59.526 31.684 18.673  1.00 37.93 ? 83  SER   A CA   1 
ATOM   370  C  C    . SER   A 1 52  ? -58.281 32.321 19.300  1.00 42.42 ? 83  SER   A C    1 
ATOM   371  O  O    . SER   A 1 52  ? -58.228 32.549 20.519  1.00 37.27 ? 83  SER   A O    1 
ATOM   372  C  CB   . SER   A 1 52  ? -59.288 30.213 18.327  1.00 40.74 ? 83  SER   A CB   1 
ATOM   373  O  OG   . SER   A 1 52  ? -58.918 29.481 19.480  1.00 60.81 ? 83  SER   A OG   1 
ATOM   374  N  N    . TYR   A 1 53  ? -57.273 32.641 18.474  1.00 39.79 ? 84  TYR   A N    1 
ATOM   375  C  CA   . TYR   A 1 53  ? -56.018 33.165 19.007  1.00 38.71 ? 84  TYR   A CA   1 
ATOM   376  C  C    . TYR   A 1 53  ? -56.209 34.545 19.614  1.00 37.99 ? 84  TYR   A C    1 
ATOM   377  O  O    . TYR   A 1 53  ? -55.633 34.850 20.667  1.00 36.79 ? 84  TYR   A O    1 
ATOM   378  C  CB   . TYR   A 1 53  ? -54.947 33.223 17.920  1.00 36.74 ? 84  TYR   A CB   1 
ATOM   379  C  CG   . TYR   A 1 53  ? -54.664 31.897 17.267  1.00 40.95 ? 84  TYR   A CG   1 
ATOM   380  C  CD1  . TYR   A 1 53  ? -54.963 30.706 17.906  1.00 42.06 ? 84  TYR   A CD1  1 
ATOM   381  C  CD2  . TYR   A 1 53  ? -54.094 31.841 16.001  1.00 40.06 ? 84  TYR   A CD2  1 
ATOM   382  C  CE1  . TYR   A 1 53  ? -54.694 29.493 17.308  1.00 42.49 ? 84  TYR   A CE1  1 
ATOM   383  C  CE2  . TYR   A 1 53  ? -53.828 30.629 15.391  1.00 42.59 ? 84  TYR   A CE2  1 
ATOM   384  C  CZ   . TYR   A 1 53  ? -54.135 29.463 16.041  1.00 46.60 ? 84  TYR   A CZ   1 
ATOM   385  O  OH   . TYR   A 1 53  ? -53.869 28.259 15.429  1.00 46.23 ? 84  TYR   A OH   1 
ATOM   386  N  N    . VAL   A 1 54  ? -57.026 35.389 18.976  1.00 34.02 ? 85  VAL   A N    1 
ATOM   387  C  CA   . VAL   A 1 54  ? -57.298 36.703 19.546  1.00 33.19 ? 85  VAL   A CA   1 
ATOM   388  C  C    . VAL   A 1 54  ? -58.031 36.568 20.873  1.00 37.25 ? 85  VAL   A C    1 
ATOM   389  O  O    . VAL   A 1 54  ? -57.784 37.338 21.820  1.00 33.13 ? 85  VAL   A O    1 
ATOM   390  C  CB   . VAL   A 1 54  ? -58.082 37.570 18.546  1.00 34.82 ? 85  VAL   A CB   1 
ATOM   391  C  CG1  . VAL   A 1 54  ? -58.647 38.788 19.242  1.00 31.67 ? 85  VAL   A CG1  1 
ATOM   392  C  CG2  . VAL   A 1 54  ? -57.163 37.998 17.389  1.00 31.02 ? 85  VAL   A CG2  1 
ATOM   393  N  N    . LEU   A 1 55  ? -58.954 35.605 20.966  1.00 36.50 ? 86  LEU   A N    1 
ATOM   394  C  CA   . LEU   A 1 55  ? -59.652 35.400 22.237  1.00 38.26 ? 86  LEU   A CA   1 
ATOM   395  C  C    . LEU   A 1 55  ? -58.664 35.028 23.339  1.00 34.80 ? 86  LEU   A C    1 
ATOM   396  O  O    . LEU   A 1 55  ? -58.749 35.547 24.463  1.00 36.75 ? 86  LEU   A O    1 
ATOM   397  C  CB   . LEU   A 1 55  ? -60.734 34.327 22.091  1.00 38.11 ? 86  LEU   A CB   1 
ATOM   398  C  CG   . LEU   A 1 55  ? -61.462 33.917 23.386  1.00 44.32 ? 86  LEU   A CG   1 
ATOM   399  C  CD1  . LEU   A 1 55  ? -62.255 35.086 23.961  1.00 41.67 ? 86  LEU   A CD1  1 
ATOM   400  C  CD2  . LEU   A 1 55  ? -62.363 32.694 23.169  1.00 43.54 ? 86  LEU   A CD2  1 
ATOM   401  N  N    . ASN   A 1 56  ? -57.703 34.152 23.027  1.00 35.42 ? 87  ASN   A N    1 
ATOM   402  C  CA   . ASN   A 1 56  ? -56.653 33.818 23.987  1.00 37.61 ? 87  ASN   A CA   1 
ATOM   403  C  C    . ASN   A 1 56  ? -55.845 35.045 24.393  1.00 35.92 ? 87  ASN   A C    1 
ATOM   404  O  O    . ASN   A 1 56  ? -55.414 35.153 25.553  1.00 33.00 ? 87  ASN   A O    1 
ATOM   405  C  CB   . ASN   A 1 56  ? -55.749 32.726 23.411  1.00 38.50 ? 87  ASN   A CB   1 
ATOM   406  C  CG   . ASN   A 1 56  ? -56.477 31.408 23.275  1.00 42.72 ? 87  ASN   A CG   1 
ATOM   407  O  OD1  . ASN   A 1 56  ? -57.518 31.211 23.905  1.00 44.12 ? 87  ASN   A OD1  1 
ATOM   408  N  ND2  . ASN   A 1 56  ? -55.951 30.501 22.448  1.00 42.79 ? 87  ASN   A ND2  1 
ATOM   409  N  N    . LYS   A 1 57  ? -55.619 35.980 23.452  1.00 30.34 ? 88  LYS   A N    1 
ATOM   410  C  CA   . LYS   A 1 57  ? -54.899 37.210 23.778  1.00 30.00 ? 88  LYS   A CA   1 
ATOM   411  C  C    . LYS   A 1 57  ? -55.710 38.103 24.710  1.00 36.17 ? 88  LYS   A C    1 
ATOM   412  O  O    . LYS   A 1 57  ? -55.163 38.666 25.666  1.00 36.11 ? 88  LYS   A O    1 
ATOM   413  C  CB   . LYS   A 1 57  ? -54.534 37.976 22.499  1.00 32.36 ? 88  LYS   A CB   1 
ATOM   414  C  CG   . LYS   A 1 57  ? -53.452 37.301 21.681  1.00 29.10 ? 88  LYS   A CG   1 
ATOM   415  C  CD   . LYS   A 1 57  ? -53.279 37.943 20.261  1.00 27.04 ? 88  LYS   A CD   1 
ATOM   416  C  CE   . LYS   A 1 57  ? -52.466 36.987 19.398  1.00 28.34 ? 88  LYS   A CE   1 
ATOM   417  N  NZ   . LYS   A 1 57  ? -51.920 37.598 18.131  1.00 30.47 ? 88  LYS   A NZ   1 
ATOM   418  N  N    . THR   A 1 58  ? -57.011 38.261 24.444  1.00 33.85 ? 89  THR   A N    1 
ATOM   419  C  CA   . THR   A 1 58  ? -57.833 39.116 25.300  1.00 33.38 ? 89  THR   A CA   1 
ATOM   420  C  C    . THR   A 1 58  ? -58.113 38.458 26.652  1.00 32.89 ? 89  THR   A C    1 
ATOM   421  O  O    . THR   A 1 58  ? -58.247 39.164 27.659  1.00 33.64 ? 89  THR   A O    1 
ATOM   422  C  CB   . THR   A 1 58  ? -59.144 39.478 24.593  1.00 38.54 ? 89  THR   A CB   1 
ATOM   423  O  OG1  . THR   A 1 58  ? -59.713 38.302 24.000  1.00 36.34 ? 89  THR   A OG1  1 
ATOM   424  C  CG2  . THR   A 1 58  ? -58.896 40.510 23.503  1.00 38.65 ? 89  THR   A CG2  1 
ATOM   425  N  N    . ARG   A 1 59  ? -58.202 37.124 26.696  1.00 31.24 ? 90  ARG   A N    1 
ATOM   426  C  CA   . ARG   A 1 59  ? -58.256 36.422 27.978  1.00 38.50 ? 90  ARG   A CA   1 
ATOM   427  C  C    . ARG   A 1 59  ? -57.005 36.705 28.804  1.00 35.52 ? 90  ARG   A C    1 
ATOM   428  O  O    . ARG   A 1 59  ? -57.091 37.034 29.991  1.00 38.14 ? 90  ARG   A O    1 
ATOM   429  C  CB   . ARG   A 1 59  ? -58.404 34.915 27.761  1.00 36.74 ? 90  ARG   A CB   1 
ATOM   430  C  CG   . ARG   A 1 59  ? -59.815 34.411 27.465  1.00 36.51 ? 90  ARG   A CG   1 
ATOM   431  C  CD   . ARG   A 1 59  ? -59.735 33.015 26.846  1.00 40.48 ? 90  ARG   A CD   1 
ATOM   432  N  NE   . ARG   A 1 59  ? -61.042 32.390 26.687  1.00 43.54 ? 90  ARG   A NE   1 
ATOM   433  C  CZ   . ARG   A 1 59  ? -61.214 31.141 26.272  1.00 50.44 ? 90  ARG   A CZ   1 
ATOM   434  N  NH1  . ARG   A 1 59  ? -60.185 30.384 25.928  1.00 53.32 ? 90  ARG   A NH1  1 
ATOM   435  N  NH2  . ARG   A 1 59  ? -62.446 30.635 26.210  1.00 45.44 ? 90  ARG   A NH2  1 
ATOM   436  N  N    . ALA   A 1 60  ? -55.826 36.594 28.182  1.00 31.41 ? 91  ALA   A N    1 
ATOM   437  C  CA   . ALA   A 1 60  ? -54.584 36.804 28.910  1.00 34.51 ? 91  ALA   A CA   1 
ATOM   438  C  C    . ALA   A 1 60  ? -54.458 38.243 29.361  1.00 37.88 ? 91  ALA   A C    1 
ATOM   439  O  O    . ALA   A 1 60  ? -53.936 38.509 30.454  1.00 35.96 ? 91  ALA   A O    1 
ATOM   440  C  CB   . ALA   A 1 60  ? -53.379 36.406 28.071  1.00 30.91 ? 91  ALA   A CB   1 
ATOM   441  N  N    . ALA   A 1 61  ? -54.940 39.183 28.543  1.00 32.27 ? 92  ALA   A N    1 
ATOM   442  C  CA   . ALA   A 1 61  ? -54.970 40.573 28.971  1.00 29.96 ? 92  ALA   A CA   1 
ATOM   443  C  C    . ALA   A 1 61  ? -55.725 40.713 30.290  1.00 35.34 ? 92  ALA   A C    1 
ATOM   444  O  O    . ALA   A 1 61  ? -55.229 41.338 31.237  1.00 35.71 ? 92  ALA   A O    1 
ATOM   445  C  CB   . ALA   A 1 61  ? -55.605 41.449 27.899  1.00 29.35 ? 92  ALA   A CB   1 
ATOM   446  N  N    . ALA   A 1 62  ? -56.926 40.127 30.373  1.00 33.38 ? 93  ALA   A N    1 
ATOM   447  C  CA   . ALA   A 1 62  ? -57.704 40.238 31.612  1.00 39.52 ? 93  ALA   A CA   1 
ATOM   448  C  C    . ALA   A 1 62  ? -56.942 39.634 32.786  1.00 34.49 ? 93  ALA   A C    1 
ATOM   449  O  O    . ALA   A 1 62  ? -56.883 40.226 33.868  1.00 41.65 ? 93  ALA   A O    1 
ATOM   450  C  CB   . ALA   A 1 62  ? -59.067 39.563 31.441  1.00 38.56 ? 93  ALA   A CB   1 
ATOM   451  N  N    . VAL   A 1 63  ? -56.302 38.483 32.566  1.00 33.32 ? 94  VAL   A N    1 
ATOM   452  C  CA   . VAL   A 1 63  ? -55.489 37.841 33.595  1.00 38.72 ? 94  VAL   A CA   1 
ATOM   453  C  C    . VAL   A 1 63  ? -54.425 38.785 34.160  1.00 40.36 ? 94  VAL   A C    1 
ATOM   454  O  O    . VAL   A 1 63  ? -54.205 38.831 35.377  1.00 38.47 ? 94  VAL   A O    1 
ATOM   455  C  CB   . VAL   A 1 63  ? -54.855 36.552 33.043  1.00 36.49 ? 94  VAL   A CB   1 
ATOM   456  C  CG1  . VAL   A 1 63  ? -53.792 36.032 34.018  1.00 44.59 ? 94  VAL   A CG1  1 
ATOM   457  C  CG2  . VAL   A 1 63  ? -55.925 35.498 32.835  1.00 34.51 ? 94  VAL   A CG2  1 
ATOM   458  N  N    . VAL   A 1 64  ? -53.727 39.537 33.308  1.00 33.29 ? 95  VAL   A N    1 
ATOM   459  C  CA   . VAL   A 1 64  ? -52.594 40.326 33.793  1.00 34.29 ? 95  VAL   A CA   1 
ATOM   460  C  C    . VAL   A 1 64  ? -52.991 41.761 34.120  1.00 35.85 ? 95  VAL   A C    1 
ATOM   461  O  O    . VAL   A 1 64  ? -52.121 42.597 34.395  1.00 33.77 ? 95  VAL   A O    1 
ATOM   462  C  CB   . VAL   A 1 64  ? -51.410 40.278 32.813  1.00 34.56 ? 95  VAL   A CB   1 
ATOM   463  C  CG1  . VAL   A 1 64  ? -51.061 38.832 32.492  1.00 32.85 ? 95  VAL   A CG1  1 
ATOM   464  C  CG2  . VAL   A 1 64  ? -51.726 41.053 31.540  1.00 35.33 ? 95  VAL   A CG2  1 
ATOM   465  N  N    . GLY   A 1 65  ? -54.289 42.064 34.130  1.00 37.25 ? 96  GLY   A N    1 
ATOM   466  C  CA   . GLY   A 1 65  ? -54.733 43.390 34.503  1.00 32.22 ? 96  GLY   A CA   1 
ATOM   467  C  C    . GLY   A 1 65  ? -54.600 44.449 33.441  1.00 37.78 ? 96  GLY   A C    1 
ATOM   468  O  O    . GLY   A 1 65  ? -54.539 45.638 33.775  1.00 36.41 ? 96  GLY   A O    1 
ATOM   469  N  N    . ILE   A 1 66  ? -54.555 44.060 32.164  1.00 35.76 ? 97  ILE   A N    1 
ATOM   470  C  CA   . ILE   A 1 66  ? -54.502 45.000 31.049  1.00 35.39 ? 97  ILE   A CA   1 
ATOM   471  C  C    . ILE   A 1 66  ? -55.899 45.096 30.450  1.00 29.63 ? 97  ILE   A C    1 
ATOM   472  O  O    . ILE   A 1 66  ? -56.549 44.076 30.215  1.00 31.35 ? 97  ILE   A O    1 
ATOM   473  C  CB   . ILE   A 1 66  ? -53.468 44.551 30.000  1.00 33.90 ? 97  ILE   A CB   1 
ATOM   474  C  CG1  . ILE   A 1 66  ? -52.046 44.796 30.518  1.00 34.92 ? 97  ILE   A CG1  1 
ATOM   475  C  CG2  . ILE   A 1 66  ? -53.676 45.283 28.675  1.00 31.78 ? 97  ILE   A CG2  1 
ATOM   476  C  CD1  . ILE   A 1 66  ? -50.954 44.088 29.686  1.00 30.32 ? 97  ILE   A CD1  1 
ATOM   477  N  N    . ASN   A 1 67  ? -56.398 46.312 30.281  1.00 32.36 ? 98  ASN   A N    1 
ATOM   478  C  CA   . ASN   A 1 67  ? -57.680 46.462 29.618  1.00 35.45 ? 98  ASN   A CA   1 
ATOM   479  C  C    . ASN   A 1 67  ? -57.505 46.127 28.143  1.00 36.16 ? 98  ASN   A C    1 
ATOM   480  O  O    . ASN   A 1 67  ? -56.413 46.266 27.588  1.00 35.67 ? 98  ASN   A O    1 
ATOM   481  C  CB   . ASN   A 1 67  ? -58.213 47.883 29.784  1.00 37.20 ? 98  ASN   A CB   1 
ATOM   482  C  CG   . ASN   A 1 67  ? -58.599 48.191 31.220  1.00 41.08 ? 98  ASN   A CG   1 
ATOM   483  O  OD1  . ASN   A 1 67  ? -59.056 47.313 31.945  1.00 37.27 ? 98  ASN   A OD1  1 
ATOM   484  N  ND2  . ASN   A 1 67  ? -58.407 49.436 31.635  1.00 37.71 ? 98  ASN   A ND2  1 
ATOM   485  N  N    . SER   A 1 68  ? -58.579 45.658 27.511  1.00 36.03 ? 99  SER   A N    1 
ATOM   486  C  CA   . SER   A 1 68  ? -58.491 45.335 26.094  1.00 36.34 ? 99  SER   A CA   1 
ATOM   487  C  C    . SER   A 1 68  ? -59.841 45.503 25.411  1.00 40.26 ? 99  SER   A C    1 
ATOM   488  O  O    . SER   A 1 68  ? -60.894 45.635 26.046  1.00 35.88 ? 99  SER   A O    1 
ATOM   489  C  CB   . SER   A 1 68  ? -57.975 43.912 25.869  1.00 36.77 ? 99  SER   A CB   1 
ATOM   490  O  OG   . SER   A 1 68  ? -59.003 42.948 26.035  1.00 41.10 ? 99  SER   A OG   1 
ATOM   491  N  N    . GLU   A 1 69  ? -59.781 45.507 24.086  1.00 34.19 ? 100 GLU   A N    1 
ATOM   492  C  CA   . GLU   A 1 69  ? -60.957 45.418 23.235  1.00 39.50 ? 100 GLU   A CA   1 
ATOM   493  C  C    . GLU   A 1 69  ? -60.526 44.716 21.964  1.00 40.57 ? 100 GLU   A C    1 
ATOM   494  O  O    . GLU   A 1 69  ? -59.389 44.889 21.513  1.00 36.78 ? 100 GLU   A O    1 
ATOM   495  C  CB   . GLU   A 1 69  ? -61.535 46.798 22.894  1.00 39.36 ? 100 GLU   A CB   1 
ATOM   496  C  CG   . GLU   A 1 69  ? -60.605 47.629 22.031  1.00 44.07 ? 100 GLU   A CG   1 
ATOM   497  C  CD   . GLU   A 1 69  ? -61.044 49.075 21.909  1.00 49.74 ? 100 GLU   A CD   1 
ATOM   498  O  OE1  . GLU   A 1 69  ? -62.210 49.369 22.252  1.00 49.41 ? 100 GLU   A OE1  1 
ATOM   499  O  OE2  . GLU   A 1 69  ? -60.213 49.911 21.468  1.00 49.26 ? 100 GLU   A OE2  1 
ATOM   500  N  N    . THR   A 1 70  ? -61.415 43.903 21.411  1.00 36.11 ? 101 THR   A N    1 
ATOM   501  C  CA   . THR   A 1 70  ? -61.244 43.398 20.063  1.00 38.50 ? 101 THR   A CA   1 
ATOM   502  C  C    . THR   A 1 70  ? -62.205 44.160 19.168  1.00 39.47 ? 101 THR   A C    1 
ATOM   503  O  O    . THR   A 1 70  ? -63.379 44.333 19.514  1.00 39.28 ? 101 THR   A O    1 
ATOM   504  C  CB   . THR   A 1 70  ? -61.518 41.901 19.992  1.00 39.90 ? 101 THR   A CB   1 
ATOM   505  O  OG1  . THR   A 1 70  ? -60.764 41.240 21.013  1.00 41.36 ? 101 THR   A OG1  1 
ATOM   506  C  CG2  . THR   A 1 70  ? -61.105 41.364 18.633  1.00 35.49 ? 101 THR   A CG2  1 
ATOM   507  N  N    . ILE   A 1 71  ? -61.706 44.662 18.050  1.00 39.78 ? 102 ILE   A N    1 
ATOM   508  C  CA   . ILE   A 1 71  ? -62.552 45.350 17.088  1.00 34.70 ? 102 ILE   A CA   1 
ATOM   509  C  C    . ILE   A 1 71  ? -62.604 44.470 15.851  1.00 38.51 ? 102 ILE   A C    1 
ATOM   510  O  O    . ILE   A 1 71  ? -61.613 44.356 15.115  1.00 33.67 ? 102 ILE   A O    1 
ATOM   511  C  CB   . ILE   A 1 71  ? -62.033 46.755 16.775  1.00 37.61 ? 102 ILE   A CB   1 
ATOM   512  C  CG1  . ILE   A 1 71  ? -61.876 47.541 18.079  1.00 40.58 ? 102 ILE   A CG1  1 
ATOM   513  C  CG2  . ILE   A 1 71  ? -62.988 47.470 15.845  1.00 38.27 ? 102 ILE   A CG2  1 
ATOM   514  C  CD1  . ILE   A 1 71  ? -61.016 48.769 17.940  1.00 35.75 ? 102 ILE   A CD1  1 
ATOM   515  N  N    . MET   A 1 72  ? -63.747 43.821 15.644  1.00 37.08 ? 103 MET   A N    1 
ATOM   516  C  CA   . MET   A 1 72  ? -63.929 42.918 14.517  1.00 36.86 ? 103 MET   A CA   1 
ATOM   517  C  C    . MET   A 1 72  ? -64.553 43.675 13.354  1.00 38.47 ? 103 MET   A C    1 
ATOM   518  O  O    . MET   A 1 72  ? -65.474 44.474 13.542  1.00 38.78 ? 103 MET   A O    1 
ATOM   519  C  CB   . MET   A 1 72  ? -64.803 41.726 14.907  1.00 35.42 ? 103 MET   A CB   1 
ATOM   520  N  N    . LYS   A 1 73  ? -64.022 43.442 12.157  1.00 37.42 ? 104 LYS   A N    1 
ATOM   521  C  CA   . LYS   A 1 73  ? -64.476 44.071 10.928  1.00 36.14 ? 104 LYS   A CA   1 
ATOM   522  C  C    . LYS   A 1 73  ? -64.678 42.988 9.882   1.00 39.60 ? 104 LYS   A C    1 
ATOM   523  O  O    . LYS   A 1 73  ? -64.005 41.953 9.932   1.00 38.06 ? 104 LYS   A O    1 
ATOM   524  C  CB   . LYS   A 1 73  ? -63.453 45.093 10.399  1.00 38.60 ? 104 LYS   A CB   1 
ATOM   525  C  CG   . LYS   A 1 73  ? -63.078 46.232 11.338  1.00 38.56 ? 104 LYS   A CG   1 
ATOM   526  C  CD   . LYS   A 1 73  ? -64.229 47.212 11.552  1.00 39.46 ? 104 LYS   A CD   1 
ATOM   527  C  CE   . LYS   A 1 73  ? -64.656 47.895 10.262  1.00 46.68 ? 104 LYS   A CE   1 
ATOM   528  N  NZ   . LYS   A 1 73  ? -65.658 48.986 10.515  1.00 47.84 ? 104 LYS   A NZ   1 
ATOM   529  N  N    . PRO   A 1 74  ? -65.588 43.193 8.919   1.00 40.04 ? 105 PRO   A N    1 
ATOM   530  C  CA   . PRO   A 1 74  ? -65.759 42.204 7.847   1.00 37.59 ? 105 PRO   A CA   1 
ATOM   531  C  C    . PRO   A 1 74  ? -64.566 42.205 6.913   1.00 33.83 ? 105 PRO   A C    1 
ATOM   532  O  O    . PRO   A 1 74  ? -63.886 43.218 6.743   1.00 37.09 ? 105 PRO   A O    1 
ATOM   533  C  CB   . PRO   A 1 74  ? -67.018 42.684 7.113   1.00 41.22 ? 105 PRO   A CB   1 
ATOM   534  C  CG   . PRO   A 1 74  ? -66.997 44.168 7.305   1.00 38.27 ? 105 PRO   A CG   1 
ATOM   535  C  CD   . PRO   A 1 74  ? -66.417 44.395 8.698   1.00 38.03 ? 105 PRO   A CD   1 
ATOM   536  N  N    . ALA   A 1 75  ? -64.349 41.058 6.270   1.00 36.41 ? 106 ALA   A N    1 
ATOM   537  C  CA   . ALA   A 1 75  ? -63.269 40.912 5.301   1.00 40.26 ? 106 ALA   A CA   1 
ATOM   538  C  C    . ALA   A 1 75  ? -63.391 41.883 4.135   1.00 39.99 ? 106 ALA   A C    1 
ATOM   539  O  O    . ALA   A 1 75  ? -62.394 42.149 3.453   1.00 41.10 ? 106 ALA   A O    1 
ATOM   540  C  CB   . ALA   A 1 75  ? -63.243 39.479 4.766   1.00 41.20 ? 106 ALA   A CB   1 
ATOM   541  N  N    . SER   A 1 76  ? -64.580 42.418 3.888   1.00 40.16 ? 107 SER   A N    1 
ATOM   542  C  CA   . SER   A 1 76  ? -64.785 43.293 2.738   1.00 43.31 ? 107 SER   A CA   1 
ATOM   543  C  C    . SER   A 1 76  ? -64.361 44.725 3.016   1.00 47.04 ? 107 SER   A C    1 
ATOM   544  O  O    . SER   A 1 76  ? -64.478 45.568 2.119   1.00 39.25 ? 107 SER   A O    1 
ATOM   545  C  CB   . SER   A 1 76  ? -66.252 43.273 2.306   1.00 40.31 ? 107 SER   A CB   1 
ATOM   546  O  OG   . SER   A 1 76  ? -67.109 43.465 3.431   1.00 42.51 ? 107 SER   A OG   1 
ATOM   547  N  N    . ILE   A 1 77  ? -63.897 45.019 4.236   1.00 35.11 ? 108 ILE   A N    1 
ATOM   548  C  CA   . ILE   A 1 77  ? -63.351 46.341 4.526   1.00 38.60 ? 108 ILE   A CA   1 
ATOM   549  C  C    . ILE   A 1 77  ? -62.255 46.673 3.506   1.00 41.03 ? 108 ILE   A C    1 
ATOM   550  O  O    . ILE   A 1 77  ? -61.519 45.793 3.048   1.00 40.52 ? 108 ILE   A O    1 
ATOM   551  C  CB   . ILE   A 1 77  ? -62.835 46.379 5.981   1.00 39.43 ? 108 ILE   A CB   1 
ATOM   552  C  CG1  . ILE   A 1 77  ? -62.346 47.759 6.385   1.00 42.30 ? 108 ILE   A CG1  1 
ATOM   553  C  CG2  . ILE   A 1 77  ? -61.680 45.423 6.191   1.00 39.13 ? 108 ILE   A CG2  1 
ATOM   554  C  CD1  . ILE   A 1 77  ? -61.846 47.771 7.857   1.00 42.55 ? 108 ILE   A CD1  1 
ATOM   555  N  N    . SER   A 1 78  ? -62.169 47.944 3.124   1.00 38.70 ? 109 SER   A N    1 
ATOM   556  C  CA   . SER   A 1 78  ? -61.080 48.362 2.261   1.00 36.96 ? 109 SER   A CA   1 
ATOM   557  C  C    . SER   A 1 78  ? -59.835 48.676 3.080   1.00 39.23 ? 109 SER   A C    1 
ATOM   558  O  O    . SER   A 1 78  ? -59.896 48.964 4.282   1.00 39.88 ? 109 SER   A O    1 
ATOM   559  C  CB   . SER   A 1 78  ? -61.464 49.600 1.448   1.00 41.16 ? 109 SER   A CB   1 
ATOM   560  O  OG   . SER   A 1 78  ? -61.232 50.785 2.193   1.00 43.69 ? 109 SER   A OG   1 
ATOM   561  N  N    . GLU   A 1 79  ? -58.697 48.676 2.392   1.00 35.94 ? 110 GLU   A N    1 
ATOM   562  C  CA   . GLU   A 1 79  ? -57.445 49.034 3.042   1.00 39.68 ? 110 GLU   A CA   1 
ATOM   563  C  C    . GLU   A 1 79  ? -57.506 50.446 3.608   1.00 41.32 ? 110 GLU   A C    1 
ATOM   564  O  O    . GLU   A 1 79  ? -57.063 50.681 4.740   1.00 39.86 ? 110 GLU   A O    1 
ATOM   565  C  CB   . GLU   A 1 79  ? -56.287 48.887 2.060   1.00 44.05 ? 110 GLU   A CB   1 
ATOM   566  C  CG   . GLU   A 1 79  ? -54.954 49.322 2.613   1.00 39.03 ? 110 GLU   A CG   1 
ATOM   567  C  CD   . GLU   A 1 79  ? -53.846 49.124 1.603   1.00 42.50 ? 110 GLU   A CD   1 
ATOM   568  O  OE1  . GLU   A 1 79  ? -53.595 47.963 1.215   1.00 39.56 ? 110 GLU   A OE1  1 
ATOM   569  O  OE2  . GLU   A 1 79  ? -53.253 50.137 1.178   1.00 46.49 ? 110 GLU   A OE2  1 
ATOM   570  N  N    . GLU   A 1 80  ? -58.077 51.398 2.859   1.00 36.21 ? 111 GLU   A N    1 
ATOM   571  C  CA   . GLU   A 1 80  ? -58.176 52.754 3.398   1.00 44.10 ? 111 GLU   A CA   1 
ATOM   572  C  C    . GLU   A 1 80  ? -59.035 52.791 4.661   1.00 41.27 ? 111 GLU   A C    1 
ATOM   573  O  O    . GLU   A 1 80  ? -58.734 53.532 5.603   1.00 39.97 ? 111 GLU   A O    1 
ATOM   574  C  CB   . GLU   A 1 80  ? -58.722 53.728 2.352   1.00 46.85 ? 111 GLU   A CB   1 
ATOM   575  C  CG   . GLU   A 1 80  ? -57.643 54.484 1.563   1.00 54.25 ? 111 GLU   A CG   1 
ATOM   576  C  CD   . GLU   A 1 80  ? -56.494 55.006 2.433   1.00 63.07 ? 111 GLU   A CD   1 
ATOM   577  O  OE1  . GLU   A 1 80  ? -55.317 54.820 2.037   1.00 64.98 ? 111 GLU   A OE1  1 
ATOM   578  O  OE2  . GLU   A 1 80  ? -56.761 55.603 3.509   1.00 65.86 ? 111 GLU   A OE2  1 
ATOM   579  N  N    . GLU   A 1 81  ? -60.110 52.001 4.704   1.00 38.91 ? 112 GLU   A N    1 
ATOM   580  C  CA   . GLU   A 1 81  ? -60.943 51.991 5.904   1.00 43.50 ? 112 GLU   A CA   1 
ATOM   581  C  C    . GLU   A 1 81  ? -60.186 51.428 7.104   1.00 39.69 ? 112 GLU   A C    1 
ATOM   582  O  O    . GLU   A 1 81  ? -60.338 51.926 8.223   1.00 41.25 ? 112 GLU   A O    1 
ATOM   583  C  CB   . GLU   A 1 81  ? -62.228 51.203 5.662   1.00 37.94 ? 112 GLU   A CB   1 
ATOM   584  C  CG   . GLU   A 1 81  ? -63.069 51.756 4.513   1.00 50.60 ? 112 GLU   A CG   1 
ATOM   585  C  CD   . GLU   A 1 81  ? -64.399 51.033 4.352   1.00 52.85 ? 112 GLU   A CD   1 
ATOM   586  O  OE1  . GLU   A 1 81  ? -64.392 49.819 4.035   1.00 48.76 ? 112 GLU   A OE1  1 
ATOM   587  O  OE2  . GLU   A 1 81  ? -65.454 51.680 4.549   1.00 64.40 ? 112 GLU   A OE2  1 
ATOM   588  N  N    . LEU   A 1 82  ? -59.391 50.375 6.896   1.00 36.77 ? 113 LEU   A N    1 
ATOM   589  C  CA   . LEU   A 1 82  ? -58.572 49.829 7.974   1.00 38.25 ? 113 LEU   A CA   1 
ATOM   590  C  C    . LEU   A 1 82  ? -57.523 50.837 8.413   1.00 39.14 ? 113 LEU   A C    1 
ATOM   591  O  O    . LEU   A 1 82  ? -57.281 51.005 9.613   1.00 39.08 ? 113 LEU   A O    1 
ATOM   592  C  CB   . LEU   A 1 82  ? -57.926 48.518 7.528   1.00 35.67 ? 113 LEU   A CB   1 
ATOM   593  C  CG   . LEU   A 1 82  ? -57.055 47.735 8.515   1.00 36.98 ? 113 LEU   A CG   1 
ATOM   594  C  CD1  . LEU   A 1 82  ? -57.736 47.560 9.887   1.00 34.26 ? 113 LEU   A CD1  1 
ATOM   595  C  CD2  . LEU   A 1 82  ? -56.727 46.380 7.916   1.00 34.85 ? 113 LEU   A CD2  1 
ATOM   596  N  N    . LEU   A 1 83  ? -56.911 51.534 7.450   1.00 36.58 ? 114 LEU   A N    1 
ATOM   597  C  CA   . LEU   A 1 83  ? -55.956 52.587 7.770   1.00 37.00 ? 114 LEU   A CA   1 
ATOM   598  C  C    . LEU   A 1 83  ? -56.597 53.693 8.601   1.00 37.83 ? 114 LEU   A C    1 
ATOM   599  O  O    . LEU   A 1 83  ? -55.962 54.240 9.509   1.00 40.17 ? 114 LEU   A O    1 
ATOM   600  C  CB   . LEU   A 1 83  ? -55.357 53.160 6.480   1.00 40.38 ? 114 LEU   A CB   1 
ATOM   601  C  CG   . LEU   A 1 83  ? -54.395 52.239 5.726   1.00 42.17 ? 114 LEU   A CG   1 
ATOM   602  C  CD1  . LEU   A 1 83  ? -53.982 52.830 4.370   1.00 43.47 ? 114 LEU   A CD1  1 
ATOM   603  C  CD2  . LEU   A 1 83  ? -53.160 51.954 6.570   1.00 38.63 ? 114 LEU   A CD2  1 
ATOM   604  N  N    . ASN   A 1 84  ? -57.848 54.046 8.305   1.00 37.41 ? 115 ASN   A N    1 
ATOM   605  C  CA   . ASN   A 1 84  ? -58.519 55.082 9.085   1.00 40.30 ? 115 ASN   A CA   1 
ATOM   606  C  C    . ASN   A 1 84  ? -58.716 54.649 10.531  1.00 39.21 ? 115 ASN   A C    1 
ATOM   607  O  O    . ASN   A 1 84  ? -58.504 55.440 11.452  1.00 39.48 ? 115 ASN   A O    1 
ATOM   608  C  CB   . ASN   A 1 84  ? -59.868 55.433 8.462   1.00 40.46 ? 115 ASN   A CB   1 
ATOM   609  C  CG   . ASN   A 1 84  ? -59.725 56.238 7.181   1.00 48.57 ? 115 ASN   A CG   1 
ATOM   610  O  OD1  . ASN   A 1 84  ? -58.780 57.018 7.019   1.00 50.89 ? 115 ASN   A OD1  1 
ATOM   611  N  ND2  . ASN   A 1 84  ? -60.660 56.046 6.262   1.00 49.98 ? 115 ASN   A ND2  1 
ATOM   612  N  N    . LEU   A 1 85  ? -59.149 53.406 10.747  1.00 37.65 ? 116 LEU   A N    1 
ATOM   613  C  CA   . LEU   A 1 85  ? -59.337 52.927 12.115  1.00 38.02 ? 116 LEU   A CA   1 
ATOM   614  C  C    . LEU   A 1 85  ? -58.013 52.901 12.866  1.00 40.85 ? 116 LEU   A C    1 
ATOM   615  O  O    . LEU   A 1 85  ? -57.954 53.242 14.055  1.00 44.52 ? 116 LEU   A O    1 
ATOM   616  C  CB   . LEU   A 1 85  ? -59.983 51.540 12.104  1.00 39.41 ? 116 LEU   A CB   1 
ATOM   617  C  CG   . LEU   A 1 85  ? -60.093 50.728 13.407  1.00 36.53 ? 116 LEU   A CG   1 
ATOM   618  C  CD1  . LEU   A 1 85  ? -60.932 51.460 14.433  1.00 36.13 ? 116 LEU   A CD1  1 
ATOM   619  C  CD2  . LEU   A 1 85  ? -60.690 49.351 13.116  1.00 35.18 ? 116 LEU   A CD2  1 
ATOM   620  N  N    . ILE   A 1 86  ? -56.940 52.495 12.187  1.00 38.71 ? 117 ILE   A N    1 
ATOM   621  C  CA   . ILE   A 1 86  ? -55.626 52.441 12.816  1.00 37.75 ? 117 ILE   A CA   1 
ATOM   622  C  C    . ILE   A 1 86  ? -55.167 53.837 13.205  1.00 40.37 ? 117 ILE   A C    1 
ATOM   623  O  O    . ILE   A 1 86  ? -54.636 54.050 14.305  1.00 39.08 ? 117 ILE   A O    1 
ATOM   624  C  CB   . ILE   A 1 86  ? -54.618 51.747 11.880  1.00 36.57 ? 117 ILE   A CB   1 
ATOM   625  C  CG1  . ILE   A 1 86  ? -54.838 50.226 11.894  1.00 36.40 ? 117 ILE   A CG1  1 
ATOM   626  C  CG2  . ILE   A 1 86  ? -53.182 52.102 12.269  1.00 37.24 ? 117 ILE   A CG2  1 
ATOM   627  C  CD1  . ILE   A 1 86  ? -54.122 49.508 10.771  1.00 38.94 ? 117 ILE   A CD1  1 
ATOM   628  N  N    . ASN   A 1 87  ? -55.362 54.808 12.311  1.00 40.20 ? 118 ASN   A N    1 
ATOM   629  C  CA   . ASN   A 1 87  ? -55.018 56.190 12.630  1.00 42.04 ? 118 ASN   A CA   1 
ATOM   630  C  C    . ASN   A 1 87  ? -55.836 56.701 13.812  1.00 42.21 ? 118 ASN   A C    1 
ATOM   631  O  O    . ASN   A 1 87  ? -55.330 57.461 14.650  1.00 41.87 ? 118 ASN   A O    1 
ATOM   632  C  CB   . ASN   A 1 87  ? -55.223 57.077 11.394  1.00 46.26 ? 118 ASN   A CB   1 
ATOM   633  C  CG   . ASN   A 1 87  ? -54.883 58.537 11.665  1.00 51.53 ? 118 ASN   A CG   1 
ATOM   634  O  OD1  . ASN   A 1 87  ? -55.773 59.362 11.891  1.00 53.57 ? 118 ASN   A OD1  1 
ATOM   635  N  ND2  . ASN   A 1 87  ? -53.586 58.855 11.676  1.00 49.60 ? 118 ASN   A ND2  1 
ATOM   636  N  N    . LYS   A 1 88  ? -57.106 56.301 13.894  1.00 42.41 ? 119 LYS   A N    1 
ATOM   637  C  CA   . LYS   A 1 88  ? -57.923 56.683 15.044  1.00 47.06 ? 119 LYS   A CA   1 
ATOM   638  C  C    . LYS   A 1 88  ? -57.311 56.157 16.334  1.00 43.43 ? 119 LYS   A C    1 
ATOM   639  O  O    . LYS   A 1 88  ? -57.132 56.904 17.308  1.00 47.13 ? 119 LYS   A O    1 
ATOM   640  C  CB   . LYS   A 1 88  ? -59.355 56.157 14.870  1.00 47.03 ? 119 LYS   A CB   1 
ATOM   641  C  CG   . LYS   A 1 88  ? -60.344 56.632 15.936  1.00 48.58 ? 119 LYS   A CG   1 
ATOM   642  C  CD   . LYS   A 1 88  ? -61.780 56.206 15.607  1.00 51.72 ? 119 LYS   A CD   1 
ATOM   643  C  CE   . LYS   A 1 88  ? -62.158 54.896 16.301  1.00 56.99 ? 119 LYS   A CE   1 
ATOM   644  N  NZ   . LYS   A 1 88  ? -63.583 54.476 16.069  1.00 58.55 ? 119 LYS   A NZ   1 
ATOM   645  N  N    . LEU   A 1 89  ? -56.941 54.874 16.340  1.00 40.63 ? 120 LEU   A N    1 
ATOM   646  C  CA   . LEU   A 1 89  ? -56.369 54.269 17.538  1.00 40.33 ? 120 LEU   A CA   1 
ATOM   647  C  C    . LEU   A 1 89  ? -54.957 54.778 17.815  1.00 42.97 ? 120 LEU   A C    1 
ATOM   648  O  O    . LEU   A 1 89  ? -54.553 54.853 18.983  1.00 42.41 ? 120 LEU   A O    1 
ATOM   649  C  CB   . LEU   A 1 89  ? -56.402 52.743 17.401  1.00 38.23 ? 120 LEU   A CB   1 
ATOM   650  C  CG   . LEU   A 1 89  ? -57.820 52.172 17.303  1.00 38.90 ? 120 LEU   A CG   1 
ATOM   651  C  CD1  . LEU   A 1 89  ? -57.822 50.738 16.815  1.00 37.19 ? 120 LEU   A CD1  1 
ATOM   652  C  CD2  . LEU   A 1 89  ? -58.546 52.270 18.646  1.00 37.60 ? 120 LEU   A CD2  1 
ATOM   653  N  N    . ASN   A 1 90  ? -54.191 55.131 16.770  1.00 39.10 ? 121 ASN   A N    1 
ATOM   654  C  CA   . ASN   A 1 90  ? -52.880 55.745 16.986  1.00 39.09 ? 121 ASN   A CA   1 
ATOM   655  C  C    . ASN   A 1 90  ? -53.001 57.030 17.799  1.00 44.18 ? 121 ASN   A C    1 
ATOM   656  O  O    . ASN   A 1 90  ? -52.132 57.345 18.623  1.00 44.41 ? 121 ASN   A O    1 
ATOM   657  C  CB   . ASN   A 1 90  ? -52.197 56.058 15.651  1.00 41.90 ? 121 ASN   A CB   1 
ATOM   658  C  CG   . ASN   A 1 90  ? -51.465 54.865 15.057  1.00 42.88 ? 121 ASN   A CG   1 
ATOM   659  O  OD1  . ASN   A 1 90  ? -51.144 53.890 15.751  1.00 39.04 ? 121 ASN   A OD1  1 
ATOM   660  N  ND2  . ASN   A 1 90  ? -51.180 54.948 13.759  1.00 41.18 ? 121 ASN   A ND2  1 
ATOM   661  N  N    . ASN   A 1 91  ? -54.063 57.791 17.564  1.00 43.59 ? 122 ASN   A N    1 
ATOM   662  C  CA   . ASN   A 1 91  ? -54.258 59.086 18.196  1.00 49.94 ? 122 ASN   A CA   1 
ATOM   663  C  C    . ASN   A 1 91  ? -55.071 59.015 19.485  1.00 48.75 ? 122 ASN   A C    1 
ATOM   664  O  O    . ASN   A 1 91  ? -55.342 60.058 20.087  1.00 56.57 ? 122 ASN   A O    1 
ATOM   665  C  CB   . ASN   A 1 91  ? -54.918 60.036 17.195  1.00 48.71 ? 122 ASN   A CB   1 
ATOM   666  C  CG   . ASN   A 1 91  ? -53.955 60.486 16.134  1.00 49.82 ? 122 ASN   A CG   1 
ATOM   667  O  OD1  . ASN   A 1 91  ? -52.819 60.842 16.439  1.00 59.44 ? 122 ASN   A OD1  1 
ATOM   668  N  ND2  . ASN   A 1 91  ? -54.380 60.442 14.876  1.00 51.62 ? 122 ASN   A ND2  1 
ATOM   669  N  N    . ASP   A 1 92  ? -55.456 57.817 19.923  1.00 44.96 ? 123 ASP   A N    1 
ATOM   670  C  CA   . ASP   A 1 92  ? -56.190 57.627 21.168  1.00 47.92 ? 123 ASP   A CA   1 
ATOM   671  C  C    . ASP   A 1 92  ? -55.175 57.347 22.275  1.00 47.77 ? 123 ASP   A C    1 
ATOM   672  O  O    . ASP   A 1 92  ? -54.600 56.257 22.341  1.00 45.09 ? 123 ASP   A O    1 
ATOM   673  C  CB   . ASP   A 1 92  ? -57.198 56.488 21.017  1.00 44.36 ? 123 ASP   A CB   1 
ATOM   674  C  CG   . ASP   A 1 92  ? -58.082 56.301 22.247  1.00 51.91 ? 123 ASP   A CG   1 
ATOM   675  O  OD1  . ASP   A 1 92  ? -57.855 56.972 23.282  1.00 51.24 ? 123 ASP   A OD1  1 
ATOM   676  O  OD2  . ASP   A 1 92  ? -59.011 55.461 22.181  1.00 51.59 ? 123 ASP   A OD2  1 
ATOM   677  N  N    . ASP   A 1 93  ? -54.959 58.329 23.151  1.00 53.51 ? 124 ASP   A N    1 
ATOM   678  C  CA   . ASP   A 1 93  ? -53.948 58.178 24.191  1.00 46.56 ? 124 ASP   A CA   1 
ATOM   679  C  C    . ASP   A 1 93  ? -54.294 57.091 25.197  1.00 49.56 ? 124 ASP   A C    1 
ATOM   680  O  O    . ASP   A 1 93  ? -53.414 56.678 25.962  1.00 48.11 ? 124 ASP   A O    1 
ATOM   681  C  CB   . ASP   A 1 93  ? -53.726 59.499 24.928  1.00 52.21 ? 124 ASP   A CB   1 
ATOM   682  C  CG   . ASP   A 1 93  ? -53.163 60.585 24.029  1.00 61.14 ? 124 ASP   A CG   1 
ATOM   683  O  OD1  . ASP   A 1 93  ? -52.343 60.252 23.146  1.00 59.48 ? 124 ASP   A OD1  1 
ATOM   684  O  OD2  . ASP   A 1 93  ? -53.530 61.771 24.210  1.00 66.65 ? 124 ASP   A OD2  1 
ATOM   685  N  N    . ASN   A 1 94  ? -55.544 56.627 25.228  1.00 46.70 ? 125 ASN   A N    1 
ATOM   686  C  CA   . ASN   A 1 94  ? -55.870 55.507 26.099  1.00 46.41 ? 125 ASN   A CA   1 
ATOM   687  C  C    . ASN   A 1 94  ? -55.329 54.186 25.564  1.00 47.43 ? 125 ASN   A C    1 
ATOM   688  O  O    . ASN   A 1 94  ? -55.160 53.240 26.343  1.00 43.86 ? 125 ASN   A O    1 
ATOM   689  C  CB   . ASN   A 1 94  ? -57.383 55.417 26.295  1.00 46.61 ? 125 ASN   A CB   1 
ATOM   690  C  CG   . ASN   A 1 94  ? -57.773 54.380 27.330  1.00 54.86 ? 125 ASN   A CG   1 
ATOM   691  O  OD1  . ASN   A 1 94  ? -57.196 54.323 28.429  1.00 53.42 ? 125 ASN   A OD1  1 
ATOM   692  N  ND2  . ASN   A 1 94  ? -58.749 53.538 26.983  1.00 51.95 ? 125 ASN   A ND2  1 
ATOM   693  N  N    . VAL   A 1 95  ? -55.054 54.095 24.262  1.00 46.19 ? 126 VAL   A N    1 
ATOM   694  C  CA   . VAL   A 1 95  ? -54.560 52.865 23.654  1.00 40.77 ? 126 VAL   A CA   1 
ATOM   695  C  C    . VAL   A 1 95  ? -53.041 52.833 23.761  1.00 38.99 ? 126 VAL   A C    1 
ATOM   696  O  O    . VAL   A 1 95  ? -52.349 53.677 23.185  1.00 39.62 ? 126 VAL   A O    1 
ATOM   697  C  CB   . VAL   A 1 95  ? -55.006 52.747 22.186  1.00 40.37 ? 126 VAL   A CB   1 
ATOM   698  C  CG1  . VAL   A 1 95  ? -54.460 51.473 21.586  1.00 37.14 ? 126 VAL   A CG1  1 
ATOM   699  C  CG2  . VAL   A 1 95  ? -56.521 52.746 22.091  1.00 41.29 ? 126 VAL   A CG2  1 
ATOM   700  N  N    . ASP   A 1 96  ? -52.520 51.851 24.488  1.00 40.06 ? 127 ASP   A N    1 
ATOM   701  C  CA   . ASP   A 1 96  ? -51.076 51.688 24.600  1.00 41.73 ? 127 ASP   A CA   1 
ATOM   702  C  C    . ASP   A 1 96  ? -50.538 50.715 23.562  1.00 39.24 ? 127 ASP   A C    1 
ATOM   703  O  O    . ASP   A 1 96  ? -49.465 50.943 22.998  1.00 39.11 ? 127 ASP   A O    1 
ATOM   704  C  CB   . ASP   A 1 96  ? -50.705 51.204 26.004  1.00 36.21 ? 127 ASP   A CB   1 
ATOM   705  C  CG   . ASP   A 1 96  ? -51.212 52.131 27.084  1.00 41.27 ? 127 ASP   A CG   1 
ATOM   706  O  OD1  . ASP   A 1 96  ? -50.749 53.289 27.152  1.00 44.55 ? 127 ASP   A OD1  1 
ATOM   707  O  OD2  . ASP   A 1 96  ? -52.098 51.713 27.848  1.00 44.03 ? 127 ASP   A OD2  1 
ATOM   708  N  N    . GLY   A 1 97  ? -51.267 49.638 23.312  1.00 35.68 ? 128 GLY   A N    1 
ATOM   709  C  CA   . GLY   A 1 97  ? -50.850 48.619 22.370  1.00 38.55 ? 128 GLY   A CA   1 
ATOM   710  C  C    . GLY   A 1 97  ? -51.895 48.423 21.288  1.00 36.76 ? 128 GLY   A C    1 
ATOM   711  O  O    . GLY   A 1 97  ? -53.096 48.400 21.565  1.00 34.39 ? 128 GLY   A O    1 
ATOM   712  N  N    . LEU   A 1 98  ? -51.431 48.253 20.064  1.00 35.49 ? 129 LEU   A N    1 
ATOM   713  C  CA   . LEU   A 1 98  ? -52.357 48.085 18.957  1.00 33.64 ? 129 LEU   A CA   1 
ATOM   714  C  C    . LEU   A 1 98  ? -51.786 47.049 18.007  1.00 35.18 ? 129 LEU   A C    1 
ATOM   715  O  O    . LEU   A 1 98  ? -50.630 47.160 17.591  1.00 31.47 ? 129 LEU   A O    1 
ATOM   716  C  CB   . LEU   A 1 98  ? -52.589 49.419 18.248  1.00 34.34 ? 129 LEU   A CB   1 
ATOM   717  C  CG   . LEU   A 1 98  ? -53.287 49.362 16.880  1.00 35.24 ? 129 LEU   A CG   1 
ATOM   718  C  CD1  . LEU   A 1 98  ? -54.713 48.840 17.004  1.00 33.16 ? 129 LEU   A CD1  1 
ATOM   719  C  CD2  . LEU   A 1 98  ? -53.284 50.748 16.268  1.00 33.27 ? 129 LEU   A CD2  1 
ATOM   720  N  N    . LEU   A 1 99  ? -52.576 46.031 17.686  1.00 33.50 ? 130 LEU   A N    1 
ATOM   721  C  CA   . LEU   A 1 99  ? -52.132 45.039 16.727  1.00 37.27 ? 130 LEU   A CA   1 
ATOM   722  C  C    . LEU   A 1 99  ? -53.280 44.664 15.801  1.00 33.10 ? 130 LEU   A C    1 
ATOM   723  O  O    . LEU   A 1 99  ? -54.460 44.731 16.167  1.00 29.41 ? 130 LEU   A O    1 
ATOM   724  C  CB   . LEU   A 1 99  ? -51.562 43.802 17.429  1.00 34.66 ? 130 LEU   A CB   1 
ATOM   725  C  CG   . LEU   A 1 99  ? -52.496 42.831 18.137  1.00 30.81 ? 130 LEU   A CG   1 
ATOM   726  C  CD1  . LEU   A 1 99  ? -52.863 41.688 17.188  1.00 31.69 ? 130 LEU   A CD1  1 
ATOM   727  C  CD2  . LEU   A 1 99  ? -51.804 42.291 19.380  1.00 34.24 ? 130 LEU   A CD2  1 
ATOM   728  N  N    . VAL   A 1 100 ? -52.919 44.281 14.587  1.00 32.68 ? 131 VAL   A N    1 
ATOM   729  C  CA   . VAL   A 1 100 ? -53.877 43.833 13.588  1.00 31.33 ? 131 VAL   A CA   1 
ATOM   730  C  C    . VAL   A 1 100 ? -53.609 42.360 13.361  1.00 30.71 ? 131 VAL   A C    1 
ATOM   731  O  O    . VAL   A 1 100 ? -52.562 41.992 12.819  1.00 30.15 ? 131 VAL   A O    1 
ATOM   732  C  CB   . VAL   A 1 100 ? -53.757 44.634 12.286  1.00 34.80 ? 131 VAL   A CB   1 
ATOM   733  C  CG1  . VAL   A 1 100 ? -54.807 44.186 11.302  1.00 27.39 ? 131 VAL   A CG1  1 
ATOM   734  C  CG2  . VAL   A 1 100 ? -53.891 46.108 12.607  1.00 31.25 ? 131 VAL   A CG2  1 
ATOM   735  N  N    . GLN   A 1 101 ? -54.542 41.508 13.781  1.00 28.76 ? 132 GLN   A N    1 
ATOM   736  C  CA   . GLN   A 1 101 ? -54.322 40.074 13.634  1.00 28.04 ? 132 GLN   A CA   1 
ATOM   737  C  C    . GLN   A 1 101 ? -54.189 39.712 12.162  1.00 34.20 ? 132 GLN   A C    1 
ATOM   738  O  O    . GLN   A 1 101 ? -55.018 40.111 11.342  1.00 31.90 ? 132 GLN   A O    1 
ATOM   739  C  CB   . GLN   A 1 101 ? -55.474 39.289 14.250  1.00 30.47 ? 132 GLN   A CB   1 
ATOM   740  C  CG   . GLN   A 1 101 ? -55.232 37.800 14.255  1.00 30.66 ? 132 GLN   A CG   1 
ATOM   741  C  CD   . GLN   A 1 101 ? -54.289 37.364 15.374  1.00 30.92 ? 132 GLN   A CD   1 
ATOM   742  O  OE1  . GLN   A 1 101 ? -53.906 38.169 16.230  1.00 30.24 ? 132 GLN   A OE1  1 
ATOM   743  N  NE2  . GLN   A 1 101 ? -53.919 36.084 15.374  1.00 30.92 ? 132 GLN   A NE2  1 
ATOM   744  N  N    . LEU   A 1 102 ? -53.155 38.910 11.838  1.00 34.03 ? 133 LEU   A N    1 
ATOM   745  C  CA   . LEU   A 1 102 ? -52.869 38.380 10.517  1.00 32.96 ? 133 LEU   A CA   1 
ATOM   746  C  C    . LEU   A 1 102 ? -53.337 36.933 10.406  1.00 33.48 ? 133 LEU   A C    1 
ATOM   747  O  O    . LEU   A 1 102 ? -53.398 36.217 11.411  1.00 34.32 ? 133 LEU   A O    1 
ATOM   748  C  CB   . LEU   A 1 102 ? -51.364 38.459 10.225  1.00 31.28 ? 133 LEU   A CB   1 
ATOM   749  C  CG   . LEU   A 1 102 ? -50.745 39.856 10.353  1.00 34.42 ? 133 LEU   A CG   1 
ATOM   750  C  CD1  . LEU   A 1 102 ? -49.276 39.869 9.892   1.00 33.74 ? 133 LEU   A CD1  1 
ATOM   751  C  CD2  . LEU   A 1 102 ? -51.575 40.914 9.631   1.00 29.35 ? 133 LEU   A CD2  1 
ATOM   752  N  N    . PRO   A 1 103 ? -53.652 36.435 9.192   1.00 35.60 ? 134 PRO   A N    1 
ATOM   753  C  CA   . PRO   A 1 103 ? -53.577 37.110 7.888   1.00 35.48 ? 134 PRO   A CA   1 
ATOM   754  C  C    . PRO   A 1 103 ? -54.759 38.017 7.600   1.00 34.57 ? 134 PRO   A C    1 
ATOM   755  O  O    . PRO   A 1 103 ? -55.843 37.821 8.144   1.00 37.56 ? 134 PRO   A O    1 
ATOM   756  C  CB   . PRO   A 1 103 ? -53.559 35.941 6.899   1.00 38.07 ? 134 PRO   A CB   1 
ATOM   757  C  CG   . PRO   A 1 103 ? -54.421 34.926 7.574   1.00 37.22 ? 134 PRO   A CG   1 
ATOM   758  C  CD   . PRO   A 1 103 ? -54.135 35.050 9.055   1.00 32.74 ? 134 PRO   A CD   1 
ATOM   759  N  N    . LEU   A 1 104 ? -54.546 38.986 6.730   1.00 33.77 ? 135 LEU   A N    1 
ATOM   760  C  CA   . LEU   A 1 104 ? -55.533 39.919 6.232   1.00 33.30 ? 135 LEU   A CA   1 
ATOM   761  C  C    . LEU   A 1 104 ? -55.983 39.504 4.831   1.00 35.43 ? 135 LEU   A C    1 
ATOM   762  O  O    . LEU   A 1 104 ? -55.298 38.739 4.148   1.00 36.03 ? 135 LEU   A O    1 
ATOM   763  C  CB   . LEU   A 1 104 ? -54.944 41.330 6.199   1.00 32.36 ? 135 LEU   A CB   1 
ATOM   764  C  CG   . LEU   A 1 104 ? -54.737 41.969 7.575   1.00 36.87 ? 135 LEU   A CG   1 
ATOM   765  C  CD1  . LEU   A 1 104 ? -53.933 43.249 7.450   1.00 34.98 ? 135 LEU   A CD1  1 
ATOM   766  C  CD2  . LEU   A 1 104 ? -56.074 42.240 8.266   1.00 33.49 ? 135 LEU   A CD2  1 
ATOM   767  N  N    . PRO   A 1 105 ? -57.136 39.980 4.367   1.00 35.70 ? 136 PRO   A N    1 
ATOM   768  C  CA   . PRO   A 1 105 ? -57.590 39.613 3.009   1.00 39.17 ? 136 PRO   A CA   1 
ATOM   769  C  C    . PRO   A 1 105 ? -56.597 40.065 1.946   1.00 37.20 ? 136 PRO   A C    1 
ATOM   770  O  O    . PRO   A 1 105 ? -55.761 40.942 2.173   1.00 36.50 ? 136 PRO   A O    1 
ATOM   771  C  CB   . PRO   A 1 105 ? -58.928 40.346 2.868   1.00 35.63 ? 136 PRO   A CB   1 
ATOM   772  C  CG   . PRO   A 1 105 ? -59.374 40.606 4.313   1.00 40.37 ? 136 PRO   A CG   1 
ATOM   773  C  CD   . PRO   A 1 105 ? -58.111 40.823 5.077   1.00 33.78 ? 136 PRO   A CD   1 
ATOM   774  N  N    . GLU   A 1 106 ? -56.698 39.444 0.761   1.00 43.39 ? 137 GLU   A N    1 
ATOM   775  C  CA   . GLU   A 1 106 ? -55.731 39.705 -0.306  1.00 41.17 ? 137 GLU   A CA   1 
ATOM   776  C  C    . GLU   A 1 106 ? -55.718 41.168 -0.729  1.00 40.62 ? 137 GLU   A C    1 
ATOM   777  O  O    . GLU   A 1 106 ? -54.664 41.698 -1.101  1.00 38.99 ? 137 GLU   A O    1 
ATOM   778  C  CB   . GLU   A 1 106 ? -56.025 38.801 -1.502  1.00 47.13 ? 137 GLU   A CB   1 
ATOM   779  C  CG   . GLU   A 1 106 ? -55.560 37.377 -1.284  1.00 51.41 ? 137 GLU   A CG   1 
ATOM   780  C  CD   . GLU   A 1 106 ? -54.075 37.208 -1.582  1.00 68.65 ? 137 GLU   A CD   1 
ATOM   781  O  OE1  . GLU   A 1 106 ? -53.281 37.121 -0.611  1.00 69.33 ? 137 GLU   A OE1  1 
ATOM   782  O  OE2  . GLU   A 1 106 ? -53.705 37.149 -2.781  1.00 74.95 ? 137 GLU   A OE2  1 
ATOM   783  N  N    . HIS   A 1 107 ? -56.858 41.847 -0.663  1.00 36.66 ? 138 HIS   A N    1 
ATOM   784  C  CA   . HIS   A 1 107 ? -56.892 43.228 -1.117  1.00 37.34 ? 138 HIS   A CA   1 
ATOM   785  C  C    . HIS   A 1 107 ? -56.299 44.216 -0.127  1.00 42.63 ? 138 HIS   A C    1 
ATOM   786  O  O    . HIS   A 1 107 ? -56.271 45.418 -0.423  1.00 39.27 ? 138 HIS   A O    1 
ATOM   787  C  CB   . HIS   A 1 107 ? -58.317 43.646 -1.444  1.00 41.55 ? 138 HIS   A CB   1 
ATOM   788  C  CG   . HIS   A 1 107 ? -59.268 43.541 -0.296  1.00 41.04 ? 138 HIS   A CG   1 
ATOM   789  N  ND1  . HIS   A 1 107 ? -59.834 42.346 0.094   1.00 40.38 ? 138 HIS   A ND1  1 
ATOM   790  C  CD2  . HIS   A 1 107 ? -59.796 44.491 0.513   1.00 36.87 ? 138 HIS   A CD2  1 
ATOM   791  C  CE1  . HIS   A 1 107 ? -60.660 42.563 1.101   1.00 40.52 ? 138 HIS   A CE1  1 
ATOM   792  N  NE2  . HIS   A 1 107 ? -60.655 43.857 1.373   1.00 39.73 ? 138 HIS   A NE2  1 
ATOM   793  N  N    . ILE   A 1 108 ? -55.828 43.760 1.032   1.00 39.22 ? 139 ILE   A N    1 
ATOM   794  C  CA   . ILE   A 1 108 ? -55.207 44.631 2.023   1.00 38.53 ? 139 ILE   A CA   1 
ATOM   795  C  C    . ILE   A 1 108 ? -53.734 44.260 2.121   1.00 37.79 ? 139 ILE   A C    1 
ATOM   796  O  O    . ILE   A 1 108 ? -53.396 43.079 2.263   1.00 40.99 ? 139 ILE   A O    1 
ATOM   797  C  CB   . ILE   A 1 108 ? -55.917 44.507 3.380   1.00 37.66 ? 139 ILE   A CB   1 
ATOM   798  C  CG1  . ILE   A 1 108 ? -57.318 45.117 3.291   1.00 36.41 ? 139 ILE   A CG1  1 
ATOM   799  C  CG2  . ILE   A 1 108 ? -55.099 45.162 4.460   1.00 37.06 ? 139 ILE   A CG2  1 
ATOM   800  C  CD1  . ILE   A 1 108 ? -58.119 44.966 4.569   1.00 40.44 ? 139 ILE   A CD1  1 
ATOM   801  N  N    . ASP   A 1 109 ? -52.857 45.257 2.008   1.00 36.43 ? 140 ASP   A N    1 
ATOM   802  C  CA   . ASP   A 1 109 ? -51.418 45.009 2.042   1.00 37.28 ? 140 ASP   A CA   1 
ATOM   803  C  C    . ASP   A 1 109 ? -50.963 44.978 3.505   1.00 37.17 ? 140 ASP   A C    1 
ATOM   804  O  O    . ASP   A 1 109 ? -51.002 46.006 4.187   1.00 35.07 ? 140 ASP   A O    1 
ATOM   805  C  CB   . ASP   A 1 109 ? -50.685 46.078 1.230   1.00 40.62 ? 140 ASP   A CB   1 
ATOM   806  C  CG   . ASP   A 1 109 ? -49.187 45.827 1.144   1.00 42.67 ? 140 ASP   A CG   1 
ATOM   807  O  OD1  . ASP   A 1 109 ? -48.690 45.500 0.046   1.00 55.03 ? 140 ASP   A OD1  1 
ATOM   808  O  OD2  . ASP   A 1 109 ? -48.491 45.969 2.163   1.00 47.91 ? 140 ASP   A OD2  1 
ATOM   809  N  N    . GLU   A 1 110 ? -50.543 43.795 3.989   1.00 35.88 ? 141 GLU   A N    1 
ATOM   810  C  CA   . GLU   A 1 110 ? -50.199 43.632 5.406   1.00 39.64 ? 141 GLU   A CA   1 
ATOM   811  C  C    . GLU   A 1 110 ? -49.042 44.527 5.807   1.00 37.60 ? 141 GLU   A C    1 
ATOM   812  O  O    . GLU   A 1 110 ? -49.004 45.034 6.934   1.00 39.12 ? 141 GLU   A O    1 
ATOM   813  C  CB   . GLU   A 1 110 ? -49.852 42.170 5.719   1.00 39.04 ? 141 GLU   A CB   1 
ATOM   814  C  CG   . GLU   A 1 110 ? -51.043 41.236 5.532   1.00 43.60 ? 141 GLU   A CG   1 
ATOM   815  C  CD   . GLU   A 1 110 ? -50.721 39.760 5.729   1.00 45.59 ? 141 GLU   A CD   1 
ATOM   816  O  OE1  . GLU   A 1 110 ? -49.553 39.427 6.051   1.00 43.27 ? 141 GLU   A OE1  1 
ATOM   817  O  OE2  . GLU   A 1 110 ? -51.655 38.933 5.557   1.00 45.10 ? 141 GLU   A OE2  1 
ATOM   818  N  N    . ARG   A 1 111 ? -48.062 44.693 4.919   1.00 36.72 ? 142 ARG   A N    1 
ATOM   819  C  CA   . ARG   A 1 111 ? -46.905 45.520 5.247   1.00 39.72 ? 142 ARG   A CA   1 
ATOM   820  C  C    . ARG   A 1 111 ? -47.297 46.979 5.409   1.00 38.21 ? 142 ARG   A C    1 
ATOM   821  O  O    . ARG   A 1 111 ? -46.826 47.656 6.330   1.00 38.61 ? 142 ARG   A O    1 
ATOM   822  C  CB   . ARG   A 1 111 ? -45.824 45.365 4.176   1.00 42.07 ? 142 ARG   A CB   1 
ATOM   823  C  CG   . ARG   A 1 111 ? -44.976 44.150 4.406   1.00 45.07 ? 142 ARG   A CG   1 
ATOM   824  C  CD   . ARG   A 1 111 ? -44.380 44.187 5.816   1.00 41.36 ? 142 ARG   A CD   1 
ATOM   825  N  NE   . ARG   A 1 111 ? -44.481 42.869 6.430   1.00 48.06 ? 142 ARG   A NE   1 
ATOM   826  C  CZ   . ARG   A 1 111 ? -44.070 42.552 7.654   1.00 52.50 ? 142 ARG   A CZ   1 
ATOM   827  N  NH1  . ARG   A 1 111 ? -43.444 43.429 8.429   1.00 49.40 ? 142 ARG   A NH1  1 
ATOM   828  N  NH2  . ARG   A 1 111 ? -44.298 41.322 8.116   1.00 51.05 ? 142 ARG   A NH2  1 
ATOM   829  N  N    . ARG   A 1 112 ? -48.152 47.487 4.523   1.00 36.59 ? 143 ARG   A N    1 
ATOM   830  C  CA   . ARG   A 1 112 ? -48.659 48.839 4.720   1.00 38.83 ? 143 ARG   A CA   1 
ATOM   831  C  C    . ARG   A 1 112 ? -49.453 48.950 6.023   1.00 34.48 ? 143 ARG   A C    1 
ATOM   832  O  O    . ARG   A 1 112 ? -49.349 49.954 6.736   1.00 36.49 ? 143 ARG   A O    1 
ATOM   833  C  CB   . ARG   A 1 112 ? -49.514 49.267 3.530   1.00 38.01 ? 143 ARG   A CB   1 
ATOM   834  C  CG   . ARG   A 1 112 ? -50.020 50.681 3.694   1.00 43.95 ? 143 ARG   A CG   1 
ATOM   835  C  CD   . ARG   A 1 112 ? -50.488 51.302 2.394   1.00 49.38 ? 143 ARG   A CD   1 
ATOM   836  N  NE   . ARG   A 1 112 ? -50.758 52.723 2.594   1.00 57.35 ? 143 ARG   A NE   1 
ATOM   837  C  CZ   . ARG   A 1 112 ? -51.732 53.394 1.991   1.00 58.81 ? 143 ARG   A CZ   1 
ATOM   838  N  NH1  . ARG   A 1 112 ? -52.554 52.804 1.139   1.00 57.73 ? 143 ARG   A NH1  1 
ATOM   839  N  NH2  . ARG   A 1 112 ? -51.903 54.685 2.270   1.00 55.42 ? 143 ARG   A NH2  1 
ATOM   840  N  N    . ILE   A 1 113 ? -50.256 47.932 6.348   1.00 34.31 ? 144 ILE   A N    1 
ATOM   841  C  CA   . ILE   A 1 113 ? -51.017 47.959 7.600   1.00 34.96 ? 144 ILE   A CA   1 
ATOM   842  C  C    . ILE   A 1 113 ? -50.071 47.934 8.798   1.00 34.76 ? 144 ILE   A C    1 
ATOM   843  O  O    . ILE   A 1 113 ? -50.208 48.726 9.734   1.00 35.44 ? 144 ILE   A O    1 
ATOM   844  C  CB   . ILE   A 1 113 ? -52.013 46.789 7.645   1.00 34.71 ? 144 ILE   A CB   1 
ATOM   845  C  CG1  . ILE   A 1 113 ? -53.107 46.984 6.584   1.00 32.87 ? 144 ILE   A CG1  1 
ATOM   846  C  CG2  . ILE   A 1 113 ? -52.577 46.583 9.075   1.00 32.11 ? 144 ILE   A CG2  1 
ATOM   847  C  CD1  . ILE   A 1 113 ? -53.830 48.299 6.695   1.00 33.62 ? 144 ILE   A CD1  1 
ATOM   848  N  N    . CYS   A 1 114 ? -49.084 47.031 8.768   1.00 36.85 ? 145 CYS   A N    1 
ATOM   849  C  CA   . CYS   A 1 114 ? -48.154 46.886 9.886   1.00 37.06 ? 145 CYS   A CA   1 
ATOM   850  C  C    . CYS   A 1 114 ? -47.340 48.159 10.087  1.00 40.19 ? 145 CYS   A C    1 
ATOM   851  O  O    . CYS   A 1 114 ? -47.060 48.548 11.225  1.00 38.93 ? 145 CYS   A O    1 
ATOM   852  C  CB   . CYS   A 1 114 ? -47.231 45.683 9.650   1.00 37.62 ? 145 CYS   A CB   1 
ATOM   853  S  SG   . CYS   A 1 114 ? -48.056 44.059 9.654   1.00 48.78 ? 145 CYS   A SG   1 
ATOM   854  N  N    . ASN   A 1 115 ? -46.953 48.827 8.992   1.00 36.90 ? 146 ASN   A N    1 
ATOM   855  C  CA   . ASN   A 1 115 ? -46.204 50.077 9.079   1.00 35.69 ? 146 ASN   A CA   1 
ATOM   856  C  C    . ASN   A 1 115 ? -47.068 51.268 9.453   1.00 34.43 ? 146 ASN   A C    1 
ATOM   857  O  O    . ASN   A 1 115 ? -46.522 52.333 9.760   1.00 37.93 ? 146 ASN   A O    1 
ATOM   858  C  CB   . ASN   A 1 115 ? -45.505 50.394 7.749   1.00 36.97 ? 146 ASN   A CB   1 
ATOM   859  C  CG   . ASN   A 1 115 ? -44.410 49.426 7.441   1.00 39.63 ? 146 ASN   A CG   1 
ATOM   860  O  OD1  . ASN   A 1 115 ? -43.859 48.808 8.355   1.00 34.70 ? 146 ASN   A OD1  1 
ATOM   861  N  ND2  . ASN   A 1 115 ? -44.089 49.262 6.141   1.00 36.66 ? 146 ASN   A ND2  1 
ATOM   862  N  N    . ALA   A 1 116 ? -48.389 51.136 9.412   1.00 33.40 ? 147 ALA   A N    1 
ATOM   863  C  CA   . ALA   A 1 116 ? -49.242 52.245 9.825   1.00 37.02 ? 147 ALA   A CA   1 
ATOM   864  C  C    . ALA   A 1 116 ? -49.474 52.283 11.332  1.00 37.02 ? 147 ALA   A C    1 
ATOM   865  O  O    . ALA   A 1 116 ? -49.889 53.322 11.858  1.00 37.99 ? 147 ALA   A O    1 
ATOM   866  C  CB   . ALA   A 1 116 ? -50.592 52.174 9.110   1.00 34.20 ? 147 ALA   A CB   1 
ATOM   867  N  N    . VAL   A 1 117 ? -49.257 51.175 12.032  1.00 35.57 ? 148 VAL   A N    1 
ATOM   868  C  CA   . VAL   A 1 117 ? -49.322 51.199 13.491  1.00 38.54 ? 148 VAL   A CA   1 
ATOM   869  C  C    . VAL   A 1 117 ? -48.195 52.073 14.022  1.00 38.29 ? 148 VAL   A C    1 
ATOM   870  O  O    . VAL   A 1 117 ? -47.026 51.885 13.663  1.00 39.73 ? 148 VAL   A O    1 
ATOM   871  C  CB   . VAL   A 1 117 ? -49.232 49.779 14.064  1.00 35.25 ? 148 VAL   A CB   1 
ATOM   872  C  CG1  . VAL   A 1 117 ? -49.264 49.828 15.616  1.00 35.10 ? 148 VAL   A CG1  1 
ATOM   873  C  CG2  . VAL   A 1 117 ? -50.372 48.912 13.517  1.00 34.11 ? 148 VAL   A CG2  1 
ATOM   874  N  N    . SER   A 1 118 ? -48.536 53.026 14.878  1.00 39.34 ? 149 SER   A N    1 
ATOM   875  C  CA   . SER   A 1 118 ? -47.517 53.893 15.448  1.00 43.08 ? 149 SER   A CA   1 
ATOM   876  C  C    . SER   A 1 118 ? -46.437 53.039 16.110  1.00 42.40 ? 149 SER   A C    1 
ATOM   877  O  O    . SER   A 1 118 ? -46.766 52.090 16.832  1.00 43.05 ? 149 SER   A O    1 
ATOM   878  C  CB   . SER   A 1 118 ? -48.131 54.857 16.464  1.00 45.73 ? 149 SER   A CB   1 
ATOM   879  O  OG   . SER   A 1 118 ? -47.182 55.205 17.463  1.00 55.58 ? 149 SER   A OG   1 
ATOM   880  N  N    . PRO   A 1 119 ? -45.154 53.300 15.841  1.00 44.91 ? 150 PRO   A N    1 
ATOM   881  C  CA   . PRO   A 1 119 ? -44.102 52.403 16.352  1.00 43.07 ? 150 PRO   A CA   1 
ATOM   882  C  C    . PRO   A 1 119 ? -44.153 52.214 17.851  1.00 41.84 ? 150 PRO   A C    1 
ATOM   883  O  O    . PRO   A 1 119 ? -43.844 51.120 18.335  1.00 41.33 ? 150 PRO   A O    1 
ATOM   884  C  CB   . PRO   A 1 119 ? -42.809 53.101 15.910  1.00 43.99 ? 150 PRO   A CB   1 
ATOM   885  C  CG   . PRO   A 1 119 ? -43.223 53.841 14.628  1.00 43.87 ? 150 PRO   A CG   1 
ATOM   886  C  CD   . PRO   A 1 119 ? -44.631 54.311 14.900  1.00 44.77 ? 150 PRO   A CD   1 
ATOM   887  N  N    . ASP   A 1 120 ? -44.548 53.246 18.599  1.00 44.56 ? 151 ASP   A N    1 
ATOM   888  C  CA   . ASP   A 1 120 ? -44.609 53.135 20.053  1.00 46.20 ? 151 ASP   A CA   1 
ATOM   889  C  C    . ASP   A 1 120 ? -45.660 52.131 20.508  1.00 44.11 ? 151 ASP   A C    1 
ATOM   890  O  O    . ASP   A 1 120 ? -45.526 51.551 21.594  1.00 40.24 ? 151 ASP   A O    1 
ATOM   891  C  CB   . ASP   A 1 120 ? -44.896 54.504 20.674  1.00 50.23 ? 151 ASP   A CB   1 
ATOM   892  C  CG   . ASP   A 1 120 ? -43.658 55.383 20.769  1.00 55.48 ? 151 ASP   A CG   1 
ATOM   893  O  OD1  . ASP   A 1 120 ? -42.555 54.946 20.360  1.00 52.55 ? 151 ASP   A OD1  1 
ATOM   894  O  OD2  . ASP   A 1 120 ? -43.799 56.520 21.269  1.00 63.06 ? 151 ASP   A OD2  1 
ATOM   895  N  N    . LYS   A 1 121 ? -46.713 51.923 19.711  1.00 39.74 ? 152 LYS   A N    1 
ATOM   896  C  CA   . LYS   A 1 121 ? -47.788 51.007 20.062  1.00 37.73 ? 152 LYS   A CA   1 
ATOM   897  C  C    . LYS   A 1 121 ? -47.651 49.649 19.393  1.00 37.20 ? 152 LYS   A C    1 
ATOM   898  O  O    . LYS   A 1 121 ? -48.506 48.785 19.597  1.00 36.60 ? 152 LYS   A O    1 
ATOM   899  C  CB   . LYS   A 1 121 ? -49.142 51.632 19.710  1.00 38.67 ? 152 LYS   A CB   1 
ATOM   900  C  CG   . LYS   A 1 121 ? -49.299 53.064 20.218  1.00 37.52 ? 152 LYS   A CG   1 
ATOM   901  C  CD   . LYS   A 1 121 ? -50.740 53.543 20.111  1.00 38.56 ? 152 LYS   A CD   1 
ATOM   902  C  CE   . LYS   A 1 121 ? -50.902 54.943 20.679  1.00 41.32 ? 152 LYS   A CE   1 
ATOM   903  N  NZ   . LYS   A 1 121 ? -52.325 55.228 21.007  1.00 42.47 ? 152 LYS   A NZ   1 
ATOM   904  N  N    . ASP   A 1 122 ? -46.584 49.434 18.623  1.00 37.89 ? 153 ASP   A N    1 
ATOM   905  C  CA   . ASP   A 1 122 ? -46.397 48.229 17.817  1.00 32.30 ? 153 ASP   A CA   1 
ATOM   906  C  C    . ASP   A 1 122 ? -45.992 47.054 18.707  1.00 35.88 ? 153 ASP   A C    1 
ATOM   907  O  O    . ASP   A 1 122 ? -44.833 46.628 18.750  1.00 39.25 ? 153 ASP   A O    1 
ATOM   908  C  CB   . ASP   A 1 122 ? -45.367 48.508 16.720  1.00 35.14 ? 153 ASP   A CB   1 
ATOM   909  C  CG   . ASP   A 1 122 ? -45.088 47.309 15.861  1.00 33.93 ? 153 ASP   A CG   1 
ATOM   910  O  OD1  . ASP   A 1 122 ? -43.923 47.145 15.417  1.00 38.45 ? 153 ASP   A OD1  1 
ATOM   911  O  OD2  . ASP   A 1 122 ? -46.022 46.513 15.638  1.00 33.13 ? 153 ASP   A OD2  1 
ATOM   912  N  N    . VAL   A 1 123 ? -46.983 46.494 19.414  1.00 33.34 ? 154 VAL   A N    1 
ATOM   913  C  CA   . VAL   A 1 123 ? -46.703 45.379 20.319  1.00 33.13 ? 154 VAL   A CA   1 
ATOM   914  C  C    . VAL   A 1 123 ? -46.385 44.092 19.564  1.00 37.62 ? 154 VAL   A C    1 
ATOM   915  O  O    . VAL   A 1 123 ? -45.871 43.141 20.173  1.00 35.61 ? 154 VAL   A O    1 
ATOM   916  C  CB   . VAL   A 1 123 ? -47.870 45.158 21.308  1.00 33.32 ? 154 VAL   A CB   1 
ATOM   917  C  CG1  . VAL   A 1 123 ? -47.982 46.341 22.273  1.00 33.09 ? 154 VAL   A CG1  1 
ATOM   918  C  CG2  . VAL   A 1 123 ? -49.187 44.968 20.563  1.00 34.08 ? 154 VAL   A CG2  1 
ATOM   919  N  N    . ASP   A 1 124 ? -46.690 44.025 18.256  1.00 29.87 ? 155 ASP   A N    1 
ATOM   920  C  CA   . ASP   A 1 124 ? -46.265 42.912 17.408  1.00 31.42 ? 155 ASP   A CA   1 
ATOM   921  C  C    . ASP   A 1 124 ? -44.789 42.987 17.030  1.00 29.33 ? 155 ASP   A C    1 
ATOM   922  O  O    . ASP   A 1 124 ? -44.201 41.965 16.691  1.00 29.26 ? 155 ASP   A O    1 
ATOM   923  C  CB   . ASP   A 1 124 ? -47.061 42.868 16.082  1.00 31.54 ? 155 ASP   A CB   1 
ATOM   924  C  CG   . ASP   A 1 124 ? -48.361 42.056 16.172  1.00 36.31 ? 155 ASP   A CG   1 
ATOM   925  O  OD1  . ASP   A 1 124 ? -48.396 40.987 16.824  1.00 31.99 ? 155 ASP   A OD1  1 
ATOM   926  O  OD2  . ASP   A 1 124 ? -49.355 42.488 15.551  1.00 37.54 ? 155 ASP   A OD2  1 
ATOM   927  N  N    . GLY   A 1 125 ? -44.181 44.164 17.058  1.00 29.76 ? 156 GLY   A N    1 
ATOM   928  C  CA   . GLY   A 1 125 ? -42.850 44.262 16.502  1.00 31.55 ? 156 GLY   A CA   1 
ATOM   929  C  C    . GLY   A 1 125 ? -42.819 44.125 14.994  1.00 32.16 ? 156 GLY   A C    1 
ATOM   930  O  O    . GLY   A 1 125 ? -41.792 43.733 14.439  1.00 33.58 ? 156 GLY   A O    1 
ATOM   931  N  N    . PHE   A 1 126 ? -43.927 44.417 14.313  1.00 30.40 ? 157 PHE   A N    1 
ATOM   932  C  CA   . PHE   A 1 126 ? -43.995 44.206 12.863  1.00 32.17 ? 157 PHE   A CA   1 
ATOM   933  C  C    . PHE   A 1 126 ? -43.665 45.460 12.055  1.00 35.61 ? 157 PHE   A C    1 
ATOM   934  O  O    . PHE   A 1 126 ? -43.445 45.358 10.840  1.00 31.39 ? 157 PHE   A O    1 
ATOM   935  C  CB   . PHE   A 1 126 ? -45.397 43.699 12.456  1.00 34.99 ? 157 PHE   A CB   1 
ATOM   936  C  CG   . PHE   A 1 126 ? -45.687 42.247 12.846  1.00 32.91 ? 157 PHE   A CG   1 
ATOM   937  C  CD1  . PHE   A 1 126 ? -44.677 41.397 13.263  1.00 34.18 ? 157 PHE   A CD1  1 
ATOM   938  C  CD2  . PHE   A 1 126 ? -46.980 41.746 12.775  1.00 32.21 ? 157 PHE   A CD2  1 
ATOM   939  C  CE1  . PHE   A 1 126 ? -44.948 40.080 13.616  1.00 36.38 ? 157 PHE   A CE1  1 
ATOM   940  C  CE2  . PHE   A 1 126 ? -47.264 40.421 13.113  1.00 32.78 ? 157 PHE   A CE2  1 
ATOM   941  C  CZ   . PHE   A 1 126 ? -46.242 39.585 13.529  1.00 36.34 ? 157 PHE   A CZ   1 
ATOM   942  N  N    . HIS   A 1 127 ? -43.641 46.634 12.682  1.00 32.91 ? 158 HIS   A N    1 
ATOM   943  C  CA   . HIS   A 1 127 ? -43.278 47.854 11.966  1.00 34.20 ? 158 HIS   A CA   1 
ATOM   944  C  C    . HIS   A 1 127 ? -41.860 47.739 11.410  1.00 34.65 ? 158 HIS   A C    1 
ATOM   945  O  O    . HIS   A 1 127 ? -40.965 47.194 12.064  1.00 34.32 ? 158 HIS   A O    1 
ATOM   946  C  CB   . HIS   A 1 127 ? -43.389 49.048 12.909  1.00 35.41 ? 158 HIS   A CB   1 
ATOM   947  C  CG   . HIS   A 1 127 ? -43.379 50.379 12.229  1.00 37.28 ? 158 HIS   A CG   1 
ATOM   948  N  ND1  . HIS   A 1 127 ? -42.216 51.033 11.885  1.00 40.83 ? 158 HIS   A ND1  1 
ATOM   949  C  CD2  . HIS   A 1 127 ? -44.395 51.205 11.877  1.00 36.65 ? 158 HIS   A CD2  1 
ATOM   950  C  CE1  . HIS   A 1 127 ? -42.518 52.193 11.326  1.00 42.80 ? 158 HIS   A CE1  1 
ATOM   951  N  NE2  . HIS   A 1 127 ? -43.833 52.322 11.315  1.00 37.42 ? 158 HIS   A NE2  1 
ATOM   952  N  N    . VAL   A 1 128 ? -41.658 48.247 10.187  1.00 32.66 ? 159 VAL   A N    1 
ATOM   953  C  CA   . VAL   A 1 128 ? -40.356 48.111 9.528   1.00 33.38 ? 159 VAL   A CA   1 
ATOM   954  C  C    . VAL   A 1 128 ? -39.213 48.633 10.399  1.00 31.88 ? 159 VAL   A C    1 
ATOM   955  O  O    . VAL   A 1 128 ? -38.115 48.077 10.373  1.00 36.04 ? 159 VAL   A O    1 
ATOM   956  C  CB   . VAL   A 1 128 ? -40.377 48.804 8.146   1.00 34.45 ? 159 VAL   A CB   1 
ATOM   957  C  CG1  . VAL   A 1 128 ? -40.601 50.303 8.287   1.00 36.39 ? 159 VAL   A CG1  1 
ATOM   958  C  CG2  . VAL   A 1 128 ? -39.091 48.489 7.374   1.00 35.56 ? 159 VAL   A CG2  1 
ATOM   959  N  N    . ILE   A 1 129 ? -39.445 49.685 11.194  1.00 35.89 ? 160 ILE   A N    1 
ATOM   960  C  CA   . ILE   A 1 129 ? -38.411 50.175 12.111  1.00 34.75 ? 160 ILE   A CA   1 
ATOM   961  C  C    . ILE   A 1 129 ? -38.071 49.119 13.160  1.00 37.07 ? 160 ILE   A C    1 
ATOM   962  O  O    . ILE   A 1 129 ? -36.901 48.921 13.508  1.00 36.37 ? 160 ILE   A O    1 
ATOM   963  C  CB   . ILE   A 1 129 ? -38.851 51.490 12.783  1.00 43.61 ? 160 ILE   A CB   1 
ATOM   964  C  CG1  . ILE   A 1 129 ? -39.236 52.542 11.747  1.00 44.17 ? 160 ILE   A CG1  1 
ATOM   965  C  CG2  . ILE   A 1 129 ? -37.746 52.017 13.685  1.00 44.74 ? 160 ILE   A CG2  1 
ATOM   966  C  CD1  . ILE   A 1 129 ? -38.080 53.106 10.990  1.00 50.06 ? 160 ILE   A CD1  1 
ATOM   967  N  N    . ASN   A 1 130 ? -39.085 48.444 13.707  1.00 34.99 ? 161 ASN   A N    1 
ATOM   968  C  CA   . ASN   A 1 130 ? -38.798 47.375 14.661  1.00 33.63 ? 161 ASN   A CA   1 
ATOM   969  C  C    . ASN   A 1 130 ? -38.098 46.208 13.988  1.00 35.32 ? 161 ASN   A C    1 
ATOM   970  O  O    . ASN   A 1 130 ? -37.206 45.593 14.580  1.00 34.01 ? 161 ASN   A O    1 
ATOM   971  C  CB   . ASN   A 1 130 ? -40.076 46.899 15.343  1.00 32.51 ? 161 ASN   A CB   1 
ATOM   972  C  CG   . ASN   A 1 130 ? -40.302 47.591 16.646  1.00 37.05 ? 161 ASN   A CG   1 
ATOM   973  O  OD1  . ASN   A 1 130 ? -39.388 47.677 17.462  1.00 38.06 ? 161 ASN   A OD1  1 
ATOM   974  N  ND2  . ASN   A 1 130 ? -41.511 48.121 16.850  1.00 36.95 ? 161 ASN   A ND2  1 
ATOM   975  N  N    . VAL   A 1 131 ? -38.493 45.881 12.755  1.00 31.16 ? 162 VAL   A N    1 
ATOM   976  C  CA   . VAL   A 1 131 ? -37.834 44.794 12.038  1.00 32.29 ? 162 VAL   A CA   1 
ATOM   977  C  C    . VAL   A 1 131 ? -36.377 45.148 11.776  1.00 29.04 ? 162 VAL   A C    1 
ATOM   978  O  O    . VAL   A 1 131 ? -35.468 44.345 12.020  1.00 31.79 ? 162 VAL   A O    1 
ATOM   979  C  CB   . VAL   A 1 131 ? -38.595 44.474 10.739  1.00 31.52 ? 162 VAL   A CB   1 
ATOM   980  C  CG1  . VAL   A 1 131 ? -37.843 43.412 9.920   1.00 29.04 ? 162 VAL   A CG1  1 
ATOM   981  C  CG2  . VAL   A 1 131 ? -40.014 44.018 11.079  1.00 31.31 ? 162 VAL   A CG2  1 
ATOM   982  N  N    . GLY   A 1 132 ? -36.131 46.364 11.287  1.00 32.73 ? 163 GLY   A N    1 
ATOM   983  C  CA   . GLY   A 1 132 ? -34.764 46.769 11.012  1.00 32.01 ? 163 GLY   A CA   1 
ATOM   984  C  C    . GLY   A 1 132 ? -33.915 46.785 12.266  1.00 31.57 ? 163 GLY   A C    1 
ATOM   985  O  O    . GLY   A 1 132 ? -32.801 46.251 12.290  1.00 32.17 ? 163 GLY   A O    1 
ATOM   986  N  N    . ARG   A 1 133 ? -34.452 47.353 13.347  1.00 31.45 ? 164 ARG   A N    1 
ATOM   987  C  CA   . ARG   A 1 133 ? -33.692 47.390 14.591  1.00 33.11 ? 164 ARG   A CA   1 
ATOM   988  C  C    . ARG   A 1 133 ? -33.394 45.976 15.088  1.00 31.79 ? 164 ARG   A C    1 
ATOM   989  O  O    . ARG   A 1 133 ? -32.271 45.684 15.518  1.00 32.84 ? 164 ARG   A O    1 
ATOM   990  C  CB   . ARG   A 1 133 ? -34.448 48.227 15.634  1.00 34.27 ? 164 ARG   A CB   1 
ATOM   991  C  CG   . ARG   A 1 133 ? -34.451 49.715 15.291  1.00 35.73 ? 164 ARG   A CG   1 
ATOM   992  C  CD   . ARG   A 1 133 ? -35.165 50.578 16.324  1.00 37.43 ? 164 ARG   A CD   1 
ATOM   993  N  NE   . ARG   A 1 133 ? -34.555 50.446 17.645  1.00 43.09 ? 164 ARG   A NE   1 
ATOM   994  C  CZ   . ARG   A 1 133 ? -33.580 51.221 18.108  1.00 43.91 ? 164 ARG   A CZ   1 
ATOM   995  N  NH1  . ARG   A 1 133 ? -33.118 52.245 17.408  1.00 44.97 ? 164 ARG   A NH1  1 
ATOM   996  N  NH2  . ARG   A 1 133 ? -33.039 50.947 19.293  1.00 41.57 ? 164 ARG   A NH2  1 
ATOM   997  N  N    . MET   A 1 134 ? -34.373 45.070 14.998  1.00 32.30 ? 165 MET   A N    1 
ATOM   998  C  CA   . MET   A 1 134 ? -34.126 43.685 15.400  1.00 34.28 ? 165 MET   A CA   1 
ATOM   999  C  C    . MET   A 1 134 ? -33.049 43.041 14.537  1.00 34.42 ? 165 MET   A C    1 
ATOM   1000 O  O    . MET   A 1 134 ? -32.210 42.285 15.040  1.00 30.68 ? 165 MET   A O    1 
ATOM   1001 C  CB   . MET   A 1 134 ? -35.407 42.856 15.320  1.00 36.39 ? 165 MET   A CB   1 
ATOM   1002 C  CG   . MET   A 1 134 ? -35.141 41.384 15.574  1.00 40.31 ? 165 MET   A CG   1 
ATOM   1003 S  SD   . MET   A 1 134 ? -36.499 40.286 15.168  1.00 44.93 ? 165 MET   A SD   1 
ATOM   1004 C  CE   . MET   A 1 134 ? -36.784 40.680 13.426  1.00 46.40 ? 165 MET   A CE   1 
ATOM   1005 N  N    . CYS   A 1 135 ? -33.079 43.299 13.222  1.00 31.81 ? 166 CYS   A N    1 
ATOM   1006 C  CA   . CYS   A 1 135 ? -32.090 42.699 12.328  1.00 31.93 ? 166 CYS   A CA   1 
ATOM   1007 C  C    . CYS   A 1 135 ? -30.694 43.276 12.531  1.00 32.21 ? 166 CYS   A C    1 
ATOM   1008 O  O    . CYS   A 1 135 ? -29.716 42.640 12.128  1.00 31.74 ? 166 CYS   A O    1 
ATOM   1009 C  CB   . CYS   A 1 135 ? -32.540 42.861 10.876  1.00 33.32 ? 166 CYS   A CB   1 
ATOM   1010 S  SG   . CYS   A 1 135 ? -33.975 41.819 10.554  1.00 39.37 ? 166 CYS   A SG   1 
ATOM   1011 N  N    . LEU   A 1 136 ? -30.578 44.422 13.201  1.00 33.66 ? 167 LEU   A N    1 
ATOM   1012 C  CA   . LEU   A 1 136 ? -29.299 45.017 13.587  1.00 36.14 ? 167 LEU   A CA   1 
ATOM   1013 C  C    . LEU   A 1 136 ? -28.930 44.758 15.054  1.00 36.36 ? 167 LEU   A C    1 
ATOM   1014 O  O    . LEU   A 1 136 ? -28.016 45.405 15.579  1.00 33.94 ? 167 LEU   A O    1 
ATOM   1015 C  CB   . LEU   A 1 136 ? -29.337 46.524 13.317  1.00 34.16 ? 167 LEU   A CB   1 
ATOM   1016 C  CG   . LEU   A 1 136 ? -29.534 46.927 11.850  1.00 38.73 ? 167 LEU   A CG   1 
ATOM   1017 C  CD1  . LEU   A 1 136 ? -29.780 48.419 11.724  1.00 36.82 ? 167 LEU   A CD1  1 
ATOM   1018 C  CD2  . LEU   A 1 136 ? -28.315 46.513 11.022  1.00 34.30 ? 167 LEU   A CD2  1 
ATOM   1019 N  N    . ASP   A 1 137 ? -29.622 43.834 15.726  1.00 38.07 ? 168 ASP   A N    1 
ATOM   1020 C  CA   . ASP   A 1 137 ? -29.397 43.523 17.146  1.00 33.80 ? 168 ASP   A CA   1 
ATOM   1021 C  C    . ASP   A 1 137 ? -29.463 44.773 18.030  1.00 38.44 ? 168 ASP   A C    1 
ATOM   1022 O  O    . ASP   A 1 137 ? -28.744 44.883 19.027  1.00 38.00 ? 168 ASP   A O    1 
ATOM   1023 C  CB   . ASP   A 1 137 ? -28.064 42.795 17.381  1.00 36.28 ? 168 ASP   A CB   1 
ATOM   1024 C  CG   . ASP   A 1 137 ? -27.830 41.636 16.412  1.00 37.09 ? 168 ASP   A CG   1 
ATOM   1025 O  OD1  . ASP   A 1 137 ? -28.830 41.087 15.898  1.00 36.38 ? 168 ASP   A OD1  1 
ATOM   1026 O  OD2  . ASP   A 1 137 ? -26.665 41.273 16.153  1.00 35.16 ? 168 ASP   A OD2  1 
ATOM   1027 N  N    . GLN   A 1 138 ? -30.324 45.721 17.684  1.00 36.85 ? 169 GLN   A N    1 
ATOM   1028 C  CA   . GLN   A 1 138 ? -30.594 46.848 18.562  1.00 38.24 ? 169 GLN   A CA   1 
ATOM   1029 C  C    . GLN   A 1 138 ? -31.820 46.560 19.421  1.00 40.91 ? 169 GLN   A C    1 
ATOM   1030 O  O    . GLN   A 1 138 ? -32.598 45.646 19.132  1.00 39.36 ? 169 GLN   A O    1 
ATOM   1031 C  CB   . GLN   A 1 138 ? -30.829 48.115 17.754  1.00 38.19 ? 169 GLN   A CB   1 
ATOM   1032 C  CG   . GLN   A 1 138 ? -29.628 48.615 17.022  1.00 39.41 ? 169 GLN   A CG   1 
ATOM   1033 C  CD   . GLN   A 1 138 ? -29.985 49.795 16.147  1.00 47.07 ? 169 GLN   A CD   1 
ATOM   1034 O  OE1  . GLN   A 1 138 ? -30.638 49.640 15.111  1.00 37.71 ? 169 GLN   A OE1  1 
ATOM   1035 N  NE2  . GLN   A 1 138 ? -29.597 50.989 16.578  1.00 51.85 ? 169 GLN   A NE2  1 
ATOM   1036 N  N    . TYR   A 1 139 ? -31.982 47.348 20.494  1.00 42.37 ? 170 TYR   A N    1 
ATOM   1037 C  CA   . TYR   A 1 139 ? -33.213 47.294 21.279  1.00 38.28 ? 170 TYR   A CA   1 
ATOM   1038 C  C    . TYR   A 1 139 ? -34.408 47.462 20.356  1.00 39.50 ? 170 TYR   A C    1 
ATOM   1039 O  O    . TYR   A 1 139 ? -34.408 48.332 19.480  1.00 39.70 ? 170 TYR   A O    1 
ATOM   1040 C  CB   . TYR   A 1 139 ? -33.239 48.397 22.341  1.00 44.64 ? 170 TYR   A CB   1 
ATOM   1041 C  CG   . TYR   A 1 139 ? -32.089 48.365 23.322  1.00 49.21 ? 170 TYR   A CG   1 
ATOM   1042 C  CD1  . TYR   A 1 139 ? -31.926 47.302 24.202  1.00 43.81 ? 170 TYR   A CD1  1 
ATOM   1043 C  CD2  . TYR   A 1 139 ? -31.169 49.410 23.373  1.00 52.70 ? 170 TYR   A CD2  1 
ATOM   1044 C  CE1  . TYR   A 1 139 ? -30.863 47.283 25.114  1.00 51.61 ? 170 TYR   A CE1  1 
ATOM   1045 C  CE2  . TYR   A 1 139 ? -30.111 49.396 24.266  1.00 52.94 ? 170 TYR   A CE2  1 
ATOM   1046 C  CZ   . TYR   A 1 139 ? -29.959 48.334 25.130  1.00 52.31 ? 170 TYR   A CZ   1 
ATOM   1047 O  OH   . TYR   A 1 139 ? -28.902 48.334 26.020  1.00 65.35 ? 170 TYR   A OH   1 
ATOM   1048 N  N    . SER   A 1 140 ? -35.411 46.604 20.525  1.00 34.49 ? 171 SER   A N    1 
ATOM   1049 C  CA   . SER   A 1 140 ? -36.581 46.662 19.660  1.00 36.68 ? 171 SER   A CA   1 
ATOM   1050 C  C    . SER   A 1 140 ? -37.733 45.969 20.364  1.00 36.72 ? 171 SER   A C    1 
ATOM   1051 O  O    . SER   A 1 140 ? -37.545 45.271 21.354  1.00 34.71 ? 171 SER   A O    1 
ATOM   1052 C  CB   . SER   A 1 140 ? -36.321 46.000 18.298  1.00 32.02 ? 171 SER   A CB   1 
ATOM   1053 O  OG   . SER   A 1 140 ? -36.312 44.589 18.451  1.00 32.43 ? 171 SER   A OG   1 
ATOM   1054 N  N    . MET   A 1 141 ? -38.931 46.162 19.834  1.00 35.19 ? 172 MET   A N    1 
ATOM   1055 C  CA   . MET   A 1 141 ? -40.068 45.349 20.249  1.00 36.28 ? 172 MET   A CA   1 
ATOM   1056 C  C    . MET   A 1 141 ? -39.996 44.025 19.489  1.00 39.27 ? 172 MET   A C    1 
ATOM   1057 O  O    . MET   A 1 141 ? -40.194 43.995 18.270  1.00 37.11 ? 172 MET   A O    1 
ATOM   1058 C  CB   . MET   A 1 141 ? -41.374 46.084 19.963  1.00 33.42 ? 172 MET   A CB   1 
ATOM   1059 C  CG   . MET   A 1 141 ? -42.574 45.402 20.544  1.00 38.86 ? 172 MET   A CG   1 
ATOM   1060 S  SD   . MET   A 1 141 ? -42.849 45.903 22.240  1.00 47.27 ? 172 MET   A SD   1 
ATOM   1061 C  CE   . MET   A 1 141 ? -43.590 47.506 21.996  1.00 40.69 ? 172 MET   A CE   1 
ATOM   1062 N  N    . LEU   A 1 142 ? -39.701 42.927 20.205  1.00 35.98 ? 173 LEU   A N    1 
ATOM   1063 C  CA   . LEU   A 1 142 ? -39.536 41.620 19.569  1.00 32.23 ? 173 LEU   A CA   1 
ATOM   1064 C  C    . LEU   A 1 142 ? -40.895 40.982 19.280  1.00 34.52 ? 173 LEU   A C    1 
ATOM   1065 O  O    . LEU   A 1 142 ? -41.792 41.015 20.137  1.00 32.48 ? 173 LEU   A O    1 
ATOM   1066 C  CB   . LEU   A 1 142 ? -38.732 40.685 20.474  1.00 33.43 ? 173 LEU   A CB   1 
ATOM   1067 C  CG   . LEU   A 1 142 ? -37.275 41.046 20.748  1.00 33.92 ? 173 LEU   A CG   1 
ATOM   1068 C  CD1  . LEU   A 1 142 ? -36.645 40.030 21.670  1.00 33.95 ? 173 LEU   A CD1  1 
ATOM   1069 C  CD2  . LEU   A 1 142 ? -36.498 41.151 19.411  1.00 32.27 ? 173 LEU   A CD2  1 
ATOM   1070 N  N    . PRO   A 1 143 ? -41.060 40.356 18.110  1.00 32.91 ? 174 PRO   A N    1 
ATOM   1071 C  CA   . PRO   A 1 143 ? -42.339 39.701 17.816  1.00 31.80 ? 174 PRO   A CA   1 
ATOM   1072 C  C    . PRO   A 1 143 ? -42.612 38.557 18.790  1.00 30.52 ? 174 PRO   A C    1 
ATOM   1073 O  O    . PRO   A 1 143 ? -41.697 37.873 19.262  1.00 30.49 ? 174 PRO   A O    1 
ATOM   1074 C  CB   . PRO   A 1 143 ? -42.179 39.216 16.364  1.00 33.14 ? 174 PRO   A CB   1 
ATOM   1075 C  CG   . PRO   A 1 143 ? -40.718 39.270 16.068  1.00 33.08 ? 174 PRO   A CG   1 
ATOM   1076 C  CD   . PRO   A 1 143 ? -40.118 40.304 16.971  1.00 33.56 ? 174 PRO   A CD   1 
ATOM   1077 N  N    . ALA   A 1 144 ? -43.898 38.379 19.111  1.00 30.89 ? 175 ALA   A N    1 
ATOM   1078 C  CA   . ALA   A 1 144 ? -44.276 37.554 20.264  1.00 28.68 ? 175 ALA   A CA   1 
ATOM   1079 C  C    . ALA   A 1 144 ? -43.892 36.092 20.060  1.00 30.94 ? 175 ALA   A C    1 
ATOM   1080 O  O    . ALA   A 1 144 ? -43.279 35.474 20.940  1.00 30.80 ? 175 ALA   A O    1 
ATOM   1081 C  CB   . ALA   A 1 144 ? -45.778 37.695 20.538  1.00 29.44 ? 175 ALA   A CB   1 
ATOM   1082 N  N    . THR   A 1 145 ? -44.223 35.513 18.903  1.00 29.79 ? 176 THR   A N    1 
ATOM   1083 C  CA   . THR   A 1 145 ? -43.929 34.089 18.730  1.00 28.02 ? 176 THR   A CA   1 
ATOM   1084 C  C    . THR   A 1 145 ? -42.433 33.798 18.744  1.00 31.89 ? 176 THR   A C    1 
ATOM   1085 O  O    . THR   A 1 145 ? -42.008 32.906 19.505  1.00 28.82 ? 176 THR   A O    1 
ATOM   1086 C  CB   . THR   A 1 145 ? -44.611 33.560 17.461  1.00 29.56 ? 176 THR   A CB   1 
ATOM   1087 O  OG1  . THR   A 1 145 ? -46.022 33.681 17.615  1.00 30.56 ? 176 THR   A OG1  1 
ATOM   1088 C  CG2  . THR   A 1 145 ? -44.279 32.105 17.246  1.00 30.59 ? 176 THR   A CG2  1 
ATOM   1089 N  N    . PRO   A 1 146 ? -41.583 34.496 17.967  1.00 29.67 ? 177 PRO   A N    1 
ATOM   1090 C  CA   . PRO   A 1 146 ? -40.131 34.265 18.101  1.00 28.94 ? 177 PRO   A CA   1 
ATOM   1091 C  C    . PRO   A 1 146 ? -39.613 34.489 19.516  1.00 27.76 ? 177 PRO   A C    1 
ATOM   1092 O  O    . PRO   A 1 146 ? -38.794 33.703 20.009  1.00 28.05 ? 177 PRO   A O    1 
ATOM   1093 C  CB   . PRO   A 1 146 ? -39.530 35.277 17.113  1.00 32.13 ? 177 PRO   A CB   1 
ATOM   1094 C  CG   . PRO   A 1 146 ? -40.608 35.480 16.096  1.00 31.01 ? 177 PRO   A CG   1 
ATOM   1095 C  CD   . PRO   A 1 146 ? -41.882 35.456 16.880  1.00 30.38 ? 177 PRO   A CD   1 
ATOM   1096 N  N    . TRP   A 1 147 ? -40.068 35.542 20.184  1.00 29.48 ? 178 TRP   A N    1 
ATOM   1097 C  CA   . TRP   A 1 147 ? -39.598 35.778 21.550  1.00 33.06 ? 178 TRP   A CA   1 
ATOM   1098 C  C    . TRP   A 1 147 ? -40.059 34.667 22.487  1.00 29.90 ? 178 TRP   A C    1 
ATOM   1099 O  O    . TRP   A 1 147 ? -39.313 34.254 23.379  1.00 33.39 ? 178 TRP   A O    1 
ATOM   1100 C  CB   . TRP   A 1 147 ? -40.060 37.150 22.037  1.00 29.50 ? 178 TRP   A CB   1 
ATOM   1101 C  CG   . TRP   A 1 147 ? -39.386 37.580 23.312  1.00 30.58 ? 178 TRP   A CG   1 
ATOM   1102 C  CD1  . TRP   A 1 147 ? -38.286 37.012 23.889  1.00 33.77 ? 178 TRP   A CD1  1 
ATOM   1103 C  CD2  . TRP   A 1 147 ? -39.775 38.663 24.168  1.00 30.29 ? 178 TRP   A CD2  1 
ATOM   1104 N  NE1  . TRP   A 1 147 ? -37.973 37.666 25.059  1.00 32.10 ? 178 TRP   A NE1  1 
ATOM   1105 C  CE2  . TRP   A 1 147 ? -38.865 38.690 25.249  1.00 32.77 ? 178 TRP   A CE2  1 
ATOM   1106 C  CE3  . TRP   A 1 147 ? -40.800 39.616 24.126  1.00 29.70 ? 178 TRP   A CE3  1 
ATOM   1107 C  CZ2  . TRP   A 1 147 ? -38.960 39.623 26.283  1.00 35.21 ? 178 TRP   A CZ2  1 
ATOM   1108 C  CZ3  . TRP   A 1 147 ? -40.886 40.548 25.158  1.00 34.43 ? 178 TRP   A CZ3  1 
ATOM   1109 C  CH2  . TRP   A 1 147 ? -39.974 40.543 26.219  1.00 33.49 ? 178 TRP   A CH2  1 
ATOM   1110 N  N    . GLY   A 1 148 ? -41.266 34.141 22.275  1.00 31.14 ? 179 GLY   A N    1 
ATOM   1111 C  CA   . GLY   A 1 148 ? -41.705 32.977 23.037  1.00 29.71 ? 179 GLY   A CA   1 
ATOM   1112 C  C    . GLY   A 1 148 ? -40.836 31.749 22.814  1.00 33.41 ? 179 GLY   A C    1 
ATOM   1113 O  O    . GLY   A 1 148 ? -40.547 31.007 23.750  1.00 31.16 ? 179 GLY   A O    1 
ATOM   1114 N  N    . VAL   A 1 149 ? -40.429 31.499 21.566  1.00 32.36 ? 180 VAL   A N    1 
ATOM   1115 C  CA   . VAL   A 1 149 ? -39.523 30.380 21.281  1.00 30.74 ? 180 VAL   A CA   1 
ATOM   1116 C  C    . VAL   A 1 149 ? -38.204 30.566 22.023  1.00 30.76 ? 180 VAL   A C    1 
ATOM   1117 O  O    . VAL   A 1 149 ? -37.665 29.634 22.630  1.00 35.61 ? 180 VAL   A O    1 
ATOM   1118 C  CB   . VAL   A 1 149 ? -39.282 30.259 19.758  1.00 29.63 ? 180 VAL   A CB   1 
ATOM   1119 C  CG1  . VAL   A 1 149 ? -38.066 29.393 19.495  1.00 31.24 ? 180 VAL   A CG1  1 
ATOM   1120 C  CG2  . VAL   A 1 149 ? -40.509 29.706 19.047  1.00 28.09 ? 180 VAL   A CG2  1 
ATOM   1121 N  N    . TRP   A 1 150 ? -37.659 31.779 21.967  1.00 32.57 ? 181 TRP   A N    1 
ATOM   1122 C  CA   . TRP   A 1 150 ? -36.426 32.093 22.677  1.00 33.52 ? 181 TRP   A CA   1 
ATOM   1123 C  C    . TRP   A 1 150 ? -36.579 31.863 24.178  1.00 36.43 ? 181 TRP   A C    1 
ATOM   1124 O  O    . TRP   A 1 150 ? -35.672 31.317 24.817  1.00 38.37 ? 181 TRP   A O    1 
ATOM   1125 C  CB   . TRP   A 1 150 ? -36.049 33.545 22.390  1.00 32.97 ? 181 TRP   A CB   1 
ATOM   1126 C  CG   . TRP   A 1 150 ? -35.004 34.131 23.259  1.00 39.20 ? 181 TRP   A CG   1 
ATOM   1127 C  CD1  . TRP   A 1 150 ? -35.185 34.737 24.484  1.00 43.05 ? 181 TRP   A CD1  1 
ATOM   1128 C  CD2  . TRP   A 1 150 ? -33.607 34.213 22.978  1.00 39.70 ? 181 TRP   A CD2  1 
ATOM   1129 N  NE1  . TRP   A 1 150 ? -33.975 35.168 24.986  1.00 43.67 ? 181 TRP   A NE1  1 
ATOM   1130 C  CE2  . TRP   A 1 150 ? -32.993 34.862 24.077  1.00 45.11 ? 181 TRP   A CE2  1 
ATOM   1131 C  CE3  . TRP   A 1 150 ? -32.811 33.786 21.921  1.00 39.18 ? 181 TRP   A CE3  1 
ATOM   1132 C  CZ2  . TRP   A 1 150 ? -31.618 35.099 24.131  1.00 44.30 ? 181 TRP   A CZ2  1 
ATOM   1133 C  CZ3  . TRP   A 1 150 ? -31.446 34.021 21.977  1.00 42.33 ? 181 TRP   A CZ3  1 
ATOM   1134 C  CH2  . TRP   A 1 150 ? -30.863 34.674 23.074  1.00 42.23 ? 181 TRP   A CH2  1 
ATOM   1135 N  N    . GLU   A 1 151 ? -37.711 32.299 24.758  1.00 33.81 ? 182 GLU   A N    1 
ATOM   1136 C  CA   . GLU   A 1 151 ? -37.938 32.169 26.201  1.00 36.02 ? 182 GLU   A CA   1 
ATOM   1137 C  C    . GLU   A 1 151 ? -38.055 30.712 26.625  1.00 37.62 ? 182 GLU   A C    1 
ATOM   1138 O  O    . GLU   A 1 151 ? -37.603 30.338 27.719  1.00 38.85 ? 182 GLU   A O    1 
ATOM   1139 C  CB   . GLU   A 1 151 ? -39.199 32.921 26.627  1.00 39.39 ? 182 GLU   A CB   1 
ATOM   1140 C  CG   . GLU   A 1 151 ? -39.021 34.401 26.951  1.00 43.43 ? 182 GLU   A CG   1 
ATOM   1141 C  CD   . GLU   A 1 151 ? -37.898 34.698 27.924  1.00 44.50 ? 182 GLU   A CD   1 
ATOM   1142 O  OE1  . GLU   A 1 151 ? -37.931 34.199 29.075  1.00 46.88 ? 182 GLU   A OE1  1 
ATOM   1143 O  OE2  . GLU   A 1 151 ? -36.981 35.451 27.530  1.00 45.76 ? 182 GLU   A OE2  1 
ATOM   1144 N  N    . ILE   A 1 152 ? -38.702 29.886 25.799  1.00 36.16 ? 183 ILE   A N    1 
ATOM   1145 C  CA   . ILE   A 1 152 ? -38.771 28.453 26.075  1.00 39.59 ? 183 ILE   A CA   1 
ATOM   1146 C  C    . ILE   A 1 152 ? -37.371 27.882 26.214  1.00 42.45 ? 183 ILE   A C    1 
ATOM   1147 O  O    . ILE   A 1 152 ? -37.083 27.105 27.133  1.00 38.95 ? 183 ILE   A O    1 
ATOM   1148 C  CB   . ILE   A 1 152 ? -39.549 27.726 24.966  1.00 36.14 ? 183 ILE   A CB   1 
ATOM   1149 C  CG1  . ILE   A 1 152 ? -41.053 27.949 25.111  1.00 35.18 ? 183 ILE   A CG1  1 
ATOM   1150 C  CG2  . ILE   A 1 152 ? -39.211 26.241 24.962  1.00 38.47 ? 183 ILE   A CG2  1 
ATOM   1151 C  CD1  . ILE   A 1 152 ? -41.826 27.522 23.838  1.00 39.17 ? 183 ILE   A CD1  1 
ATOM   1152 N  N    . ILE   A 1 153 ? -36.484 28.264 25.294  1.00 37.69 ? 184 ILE   A N    1 
ATOM   1153 C  CA   . ILE   A 1 153 ? -35.104 27.789 25.316  1.00 38.64 ? 184 ILE   A CA   1 
ATOM   1154 C  C    . ILE   A 1 153 ? -34.366 28.344 26.527  1.00 39.51 ? 184 ILE   A C    1 
ATOM   1155 O  O    . ILE   A 1 153 ? -33.722 27.599 27.274  1.00 43.14 ? 184 ILE   A O    1 
ATOM   1156 C  CB   . ILE   A 1 153 ? -34.403 28.170 23.995  1.00 39.21 ? 184 ILE   A CB   1 
ATOM   1157 C  CG1  . ILE   A 1 153 ? -35.043 27.419 22.832  1.00 38.00 ? 184 ILE   A CG1  1 
ATOM   1158 C  CG2  . ILE   A 1 153 ? -32.912 27.898 24.055  1.00 39.52 ? 184 ILE   A CG2  1 
ATOM   1159 C  CD1  . ILE   A 1 153 ? -34.576 27.893 21.443  1.00 37.69 ? 184 ILE   A CD1  1 
ATOM   1160 N  N    . LYS   A 1 154 ? -34.464 29.657 26.753  1.00 39.03 ? 185 LYS   A N    1 
ATOM   1161 C  CA   . LYS   A 1 154 ? -33.699 30.272 27.833  1.00 40.64 ? 185 LYS   A CA   1 
ATOM   1162 C  C    . LYS   A 1 154 ? -34.198 29.818 29.199  1.00 41.65 ? 185 LYS   A C    1 
ATOM   1163 O  O    . LYS   A 1 154 ? -33.405 29.404 30.055  1.00 42.15 ? 185 LYS   A O    1 
ATOM   1164 C  CB   . LYS   A 1 154 ? -33.752 31.796 27.729  1.00 42.26 ? 185 LYS   A CB   1 
ATOM   1165 C  CG   . LYS   A 1 154 ? -33.036 32.358 26.513  1.00 47.71 ? 185 LYS   A CG   1 
ATOM   1166 C  CD   . LYS   A 1 154 ? -31.570 31.924 26.480  1.00 50.25 ? 185 LYS   A CD   1 
ATOM   1167 C  CE   . LYS   A 1 154 ? -31.053 31.755 25.040  1.00 48.85 ? 185 LYS   A CE   1 
ATOM   1168 N  NZ   . LYS   A 1 154 ? -29.615 31.328 24.971  1.00 47.35 ? 185 LYS   A NZ   1 
ATOM   1169 N  N    . ARG   A 1 155 ? -35.511 29.884 29.427  1.00 40.77 ? 186 ARG   A N    1 
ATOM   1170 C  CA   . ARG   A 1 155 ? -36.032 29.508 30.738  1.00 39.01 ? 186 ARG   A CA   1 
ATOM   1171 C  C    . ARG   A 1 155 ? -35.854 28.024 31.028  1.00 41.16 ? 186 ARG   A C    1 
ATOM   1172 O  O    . ARG   A 1 155 ? -35.816 27.637 32.198  1.00 43.39 ? 186 ARG   A O    1 
ATOM   1173 C  CB   . ARG   A 1 155 ? -37.503 29.917 30.867  1.00 40.27 ? 186 ARG   A CB   1 
ATOM   1174 C  CG   . ARG   A 1 155 ? -37.661 31.430 31.081  1.00 43.31 ? 186 ARG   A CG   1 
ATOM   1175 C  CD   . ARG   A 1 155 ? -39.104 31.882 31.251  1.00 43.33 ? 186 ARG   A CD   1 
ATOM   1176 N  NE   . ARG   A 1 155 ? -39.212 33.332 31.380  1.00 44.97 ? 186 ARG   A NE   1 
ATOM   1177 C  CZ   . ARG   A 1 155 ? -39.662 33.964 32.459  1.00 45.94 ? 186 ARG   A CZ   1 
ATOM   1178 N  NH1  . ARG   A 1 155 ? -40.057 33.304 33.538  1.00 43.53 ? 186 ARG   A NH1  1 
ATOM   1179 N  NH2  . ARG   A 1 155 ? -39.743 35.292 32.446  1.00 42.12 ? 186 ARG   A NH2  1 
ATOM   1180 N  N    . THR   A 1 156 ? -35.720 27.189 30.006  1.00 40.43 ? 187 THR   A N    1 
ATOM   1181 C  CA   . THR   A 1 156 ? -35.425 25.781 30.222  1.00 40.09 ? 187 THR   A CA   1 
ATOM   1182 C  C    . THR   A 1 156 ? -33.934 25.522 30.397  1.00 43.24 ? 187 THR   A C    1 
ATOM   1183 O  O    . THR   A 1 156 ? -33.554 24.433 30.838  1.00 47.57 ? 187 THR   A O    1 
ATOM   1184 C  CB   . THR   A 1 156 ? -36.007 24.967 29.070  1.00 41.13 ? 187 THR   A CB   1 
ATOM   1185 O  OG1  . THR   A 1 156 ? -37.424 25.188 29.039  1.00 40.78 ? 187 THR   A OG1  1 
ATOM   1186 C  CG2  . THR   A 1 156 ? -35.749 23.468 29.230  1.00 48.92 ? 187 THR   A CG2  1 
ATOM   1187 N  N    . GLY   A 1 157 ? -33.083 26.510 30.132  1.00 39.57 ? 188 GLY   A N    1 
ATOM   1188 C  CA   . GLY   A 1 157 ? -31.659 26.303 30.303  1.00 44.79 ? 188 GLY   A CA   1 
ATOM   1189 C  C    . GLY   A 1 157 ? -30.982 25.522 29.195  1.00 47.25 ? 188 GLY   A C    1 
ATOM   1190 O  O    . GLY   A 1 157 ? -29.876 25.011 29.400  1.00 49.60 ? 188 GLY   A O    1 
ATOM   1191 N  N    . ILE   A 1 158 ? -31.612 25.400 28.030  1.00 46.32 ? 189 ILE   A N    1 
ATOM   1192 C  CA   . ILE   A 1 158 ? -31.010 24.732 26.875  1.00 43.83 ? 189 ILE   A CA   1 
ATOM   1193 C  C    . ILE   A 1 158 ? -29.957 25.661 26.278  1.00 47.52 ? 189 ILE   A C    1 
ATOM   1194 O  O    . ILE   A 1 158 ? -30.283 26.801 25.926  1.00 45.41 ? 189 ILE   A O    1 
ATOM   1195 C  CB   . ILE   A 1 158 ? -32.078 24.357 25.841  1.00 43.84 ? 189 ILE   A CB   1 
ATOM   1196 C  CG1  . ILE   A 1 158 ? -33.064 23.357 26.446  1.00 41.24 ? 189 ILE   A CG1  1 
ATOM   1197 C  CG2  . ILE   A 1 158 ? -31.425 23.811 24.562  1.00 40.28 ? 189 ILE   A CG2  1 
ATOM   1198 C  CD1  . ILE   A 1 158 ? -34.425 23.353 25.773  1.00 39.20 ? 189 ILE   A CD1  1 
ATOM   1199 N  N    . PRO   A 1 159 ? -28.691 25.255 26.193  1.00 49.48 ? 190 PRO   A N    1 
ATOM   1200 C  CA   . PRO   A 1 159 ? -27.665 26.170 25.678  1.00 45.84 ? 190 PRO   A CA   1 
ATOM   1201 C  C    . PRO   A 1 159 ? -27.714 26.328 24.171  1.00 44.95 ? 190 PRO   A C    1 
ATOM   1202 O  O    . PRO   A 1 159 ? -28.106 25.426 23.422  1.00 41.65 ? 190 PRO   A O    1 
ATOM   1203 C  CB   . PRO   A 1 159 ? -26.346 25.520 26.117  1.00 49.91 ? 190 PRO   A CB   1 
ATOM   1204 C  CG   . PRO   A 1 159 ? -26.694 24.089 26.421  1.00 54.87 ? 190 PRO   A CG   1 
ATOM   1205 C  CD   . PRO   A 1 159 ? -28.101 24.111 26.915  1.00 47.25 ? 190 PRO   A CD   1 
ATOM   1206 N  N    . THR   A 1 160 ? -27.282 27.504 23.730  1.00 44.15 ? 191 THR   A N    1 
ATOM   1207 C  CA   . THR   A 1 160 ? -27.285 27.832 22.316  1.00 39.93 ? 191 THR   A CA   1 
ATOM   1208 C  C    . THR   A 1 160 ? -25.931 28.242 21.761  1.00 39.44 ? 191 THR   A C    1 
ATOM   1209 O  O    . THR   A 1 160 ? -25.706 28.067 20.561  1.00 42.66 ? 191 THR   A O    1 
ATOM   1210 C  CB   . THR   A 1 160 ? -28.289 28.959 22.038  1.00 38.17 ? 191 THR   A CB   1 
ATOM   1211 O  OG1  . THR   A 1 160 ? -27.942 30.095 22.831  1.00 37.88 ? 191 THR   A OG1  1 
ATOM   1212 C  CG2  . THR   A 1 160 ? -29.695 28.515 22.391  1.00 38.49 ? 191 THR   A CG2  1 
ATOM   1213 N  N    . LEU   A 1 161 ? -25.034 28.791 22.577  1.00 40.91 ? 192 LEU   A N    1 
ATOM   1214 C  CA   . LEU   A 1 161 ? -23.780 29.308 22.045  1.00 41.16 ? 192 LEU   A CA   1 
ATOM   1215 C  C    . LEU   A 1 161 ? -22.941 28.168 21.487  1.00 44.27 ? 192 LEU   A C    1 
ATOM   1216 O  O    . LEU   A 1 161 ? -22.695 27.173 22.174  1.00 40.23 ? 192 LEU   A O    1 
ATOM   1217 C  CB   . LEU   A 1 161 ? -23.006 30.065 23.123  1.00 41.61 ? 192 LEU   A CB   1 
ATOM   1218 C  CG   . LEU   A 1 161 ? -21.741 30.796 22.659  1.00 44.06 ? 192 LEU   A CG   1 
ATOM   1219 C  CD1  . LEU   A 1 161 ? -21.505 32.014 23.516  1.00 41.37 ? 192 LEU   A CD1  1 
ATOM   1220 C  CD2  . LEU   A 1 161 ? -20.497 29.883 22.679  1.00 47.52 ? 192 LEU   A CD2  1 
ATOM   1221 N  N    . GLY   A 1 162 ? -22.501 28.319 20.236  1.00 41.83 ? 193 GLY   A N    1 
ATOM   1222 C  CA   . GLY   A 1 162 ? -21.738 27.293 19.561  1.00 42.94 ? 193 GLY   A CA   1 
ATOM   1223 C  C    . GLY   A 1 162 ? -22.524 26.066 19.164  1.00 44.54 ? 193 GLY   A C    1 
ATOM   1224 O  O    . GLY   A 1 162 ? -21.929 25.109 18.660  1.00 46.39 ? 193 GLY   A O    1 
ATOM   1225 N  N    . LYS   A 1 163 ? -23.835 26.056 19.365  1.00 43.34 ? 194 LYS   A N    1 
ATOM   1226 C  CA   . LYS   A 1 163 ? -24.645 24.884 19.067  1.00 45.93 ? 194 LYS   A CA   1 
ATOM   1227 C  C    . LYS   A 1 163 ? -25.201 24.975 17.656  1.00 45.40 ? 194 LYS   A C    1 
ATOM   1228 O  O    . LYS   A 1 163 ? -25.254 26.053 17.059  1.00 45.90 ? 194 LYS   A O    1 
ATOM   1229 C  CB   . LYS   A 1 163 ? -25.791 24.748 20.078  1.00 45.54 ? 194 LYS   A CB   1 
ATOM   1230 C  CG   . LYS   A 1 163 ? -25.344 24.824 21.540  1.00 45.74 ? 194 LYS   A CG   1 
ATOM   1231 C  CD   . LYS   A 1 163 ? -24.808 23.472 22.004  1.00 49.01 ? 194 LYS   A CD   1 
ATOM   1232 C  CE   . LYS   A 1 163 ? -24.178 23.555 23.384  1.00 53.22 ? 194 LYS   A CE   1 
ATOM   1233 N  NZ   . LYS   A 1 163 ? -22.696 23.703 23.273  1.00 61.47 ? 194 LYS   A NZ   1 
ATOM   1234 N  N    . ASN   A 1 164 ? -25.611 23.820 17.120  1.00 43.73 ? 195 ASN   A N    1 
ATOM   1235 C  CA   . ASN   A 1 164 ? -26.231 23.748 15.803  1.00 45.77 ? 195 ASN   A CA   1 
ATOM   1236 C  C    . ASN   A 1 164 ? -27.741 23.827 15.959  1.00 46.81 ? 195 ASN   A C    1 
ATOM   1237 O  O    . ASN   A 1 164 ? -28.325 23.096 16.768  1.00 46.39 ? 195 ASN   A O    1 
ATOM   1238 C  CB   . ASN   A 1 164 ? -25.859 22.452 15.078  1.00 44.84 ? 195 ASN   A CB   1 
ATOM   1239 C  CG   . ASN   A 1 164 ? -24.368 22.338 14.787  1.00 51.19 ? 195 ASN   A CG   1 
ATOM   1240 O  OD1  . ASN   A 1 164 ? -23.643 23.335 14.756  1.00 49.64 ? 195 ASN   A OD1  1 
ATOM   1241 N  ND2  . ASN   A 1 164 ? -23.906 21.109 14.564  1.00 52.99 ? 195 ASN   A ND2  1 
ATOM   1242 N  N    . VAL   A 1 165 ? -28.368 24.716 15.196  1.00 45.65 ? 196 VAL   A N    1 
ATOM   1243 C  CA   . VAL   A 1 165 ? -29.812 24.913 15.232  1.00 41.36 ? 196 VAL   A CA   1 
ATOM   1244 C  C    . VAL   A 1 165 ? -30.331 24.886 13.811  1.00 42.40 ? 196 VAL   A C    1 
ATOM   1245 O  O    . VAL   A 1 165 ? -29.741 25.508 12.921  1.00 44.52 ? 196 VAL   A O    1 
ATOM   1246 C  CB   . VAL   A 1 165 ? -30.201 26.249 15.896  1.00 38.83 ? 196 VAL   A CB   1 
ATOM   1247 C  CG1  . VAL   A 1 165 ? -31.695 26.527 15.685  1.00 37.08 ? 196 VAL   A CG1  1 
ATOM   1248 C  CG2  . VAL   A 1 165 ? -29.826 26.255 17.367  1.00 43.79 ? 196 VAL   A CG2  1 
ATOM   1249 N  N    . VAL   A 1 166 ? -31.444 24.193 13.597  1.00 39.98 ? 197 VAL   A N    1 
ATOM   1250 C  CA   . VAL   A 1 166 ? -32.135 24.201 12.315  1.00 38.31 ? 197 VAL   A CA   1 
ATOM   1251 C  C    . VAL   A 1 166 ? -33.512 24.804 12.528  1.00 40.05 ? 197 VAL   A C    1 
ATOM   1252 O  O    . VAL   A 1 166 ? -34.252 24.376 13.426  1.00 38.95 ? 197 VAL   A O    1 
ATOM   1253 C  CB   . VAL   A 1 166 ? -32.261 22.790 11.705  1.00 39.90 ? 197 VAL   A CB   1 
ATOM   1254 C  CG1  . VAL   A 1 166 ? -33.097 22.847 10.437  1.00 38.40 ? 197 VAL   A CG1  1 
ATOM   1255 C  CG2  . VAL   A 1 166 ? -30.901 22.186 11.435  1.00 40.52 ? 197 VAL   A CG2  1 
ATOM   1256 N  N    . VAL   A 1 167 ? -33.852 25.790 11.705  1.00 36.20 ? 198 VAL   A N    1 
ATOM   1257 C  CA   . VAL   A 1 167 ? -35.195 26.351 11.648  1.00 35.16 ? 198 VAL   A CA   1 
ATOM   1258 C  C    . VAL   A 1 167 ? -35.816 25.897 10.333  1.00 39.97 ? 198 VAL   A C    1 
ATOM   1259 O  O    . VAL   A 1 167 ? -35.250 26.124 9.258   1.00 38.13 ? 198 VAL   A O    1 
ATOM   1260 C  CB   . VAL   A 1 167 ? -35.173 27.888 11.756  1.00 33.97 ? 198 VAL   A CB   1 
ATOM   1261 C  CG1  . VAL   A 1 167 ? -36.590 28.453 11.819  1.00 34.09 ? 198 VAL   A CG1  1 
ATOM   1262 C  CG2  . VAL   A 1 167 ? -34.354 28.338 12.974  1.00 35.47 ? 198 VAL   A CG2  1 
ATOM   1263 N  N    . ALA   A 1 168 ? -36.972 25.251 10.409  1.00 40.76 ? 199 ALA   A N    1 
ATOM   1264 C  CA   . ALA   A 1 168 ? -37.760 24.929 9.222   1.00 40.07 ? 199 ALA   A CA   1 
ATOM   1265 C  C    . ALA   A 1 168 ? -38.850 25.983 9.094   1.00 38.12 ? 199 ALA   A C    1 
ATOM   1266 O  O    . ALA   A 1 168 ? -39.775 26.033 9.907   1.00 39.20 ? 199 ALA   A O    1 
ATOM   1267 C  CB   . ALA   A 1 168 ? -38.347 23.520 9.309   1.00 40.34 ? 199 ALA   A CB   1 
ATOM   1268 N  N    . GLY   A 1 169 ? -38.736 26.831 8.076   1.00 37.62 ? 200 GLY   A N    1 
ATOM   1269 C  CA   . GLY   A 1 169 ? -39.602 27.981 7.959   1.00 35.58 ? 200 GLY   A CA   1 
ATOM   1270 C  C    . GLY   A 1 169 ? -38.782 29.251 7.873   1.00 36.35 ? 200 GLY   A C    1 
ATOM   1271 O  O    . GLY   A 1 169 ? -37.739 29.373 8.518   1.00 35.17 ? 200 GLY   A O    1 
ATOM   1272 N  N    . ARG   A 1 170 ? -39.236 30.192 7.043   1.00 35.60 ? 201 ARG   A N    1 
ATOM   1273 C  CA   . ARG   A 1 170 ? -38.516 31.438 6.808   1.00 34.99 ? 201 ARG   A CA   1 
ATOM   1274 C  C    . ARG   A 1 170 ? -39.487 32.599 6.743   1.00 30.63 ? 201 ARG   A C    1 
ATOM   1275 O  O    . ARG   A 1 170 ? -39.146 33.654 6.198   1.00 32.42 ? 201 ARG   A O    1 
ATOM   1276 C  CB   . ARG   A 1 170 ? -37.700 31.383 5.500   1.00 35.20 ? 201 ARG   A CB   1 
ATOM   1277 C  CG   . ARG   A 1 170 ? -38.567 31.164 4.283   1.00 33.86 ? 201 ARG   A CG   1 
ATOM   1278 C  CD   . ARG   A 1 170 ? -37.789 31.228 2.930   1.00 34.73 ? 201 ARG   A CD   1 
ATOM   1279 N  NE   . ARG   A 1 170 ? -38.663 30.832 1.827   1.00 39.63 ? 201 ARG   A NE   1 
ATOM   1280 C  CZ   . ARG   A 1 170 ? -38.266 30.598 0.580   1.00 37.78 ? 201 ARG   A CZ   1 
ATOM   1281 N  NH1  . ARG   A 1 170 ? -36.995 30.698 0.225   1.00 37.31 ? 201 ARG   A NH1  1 
ATOM   1282 N  NH2  . ARG   A 1 170 ? -39.168 30.249 -0.331  1.00 36.83 ? 201 ARG   A NH2  1 
ATOM   1283 N  N    . SER   A 1 171 ? -40.701 32.416 7.251   1.00 32.80 ? 202 SER   A N    1 
ATOM   1284 C  CA   . SER   A 1 171 ? -41.689 33.480 7.202   1.00 29.92 ? 202 SER   A CA   1 
ATOM   1285 C  C    . SER   A 1 171 ? -41.182 34.693 7.968   1.00 33.21 ? 202 SER   A C    1 
ATOM   1286 O  O    . SER   A 1 171 ? -40.483 34.575 8.986   1.00 30.96 ? 202 SER   A O    1 
ATOM   1287 C  CB   . SER   A 1 171 ? -43.017 33.003 7.801   1.00 35.90 ? 202 SER   A CB   1 
ATOM   1288 O  OG   . SER   A 1 171 ? -42.911 32.881 9.223   1.00 34.30 ? 202 SER   A OG   1 
ATOM   1289 N  N    . LYS   A 1 172 ? -41.585 35.869 7.492   1.00 29.21 ? 203 LYS   A N    1 
ATOM   1290 C  CA   . LYS   A 1 172 ? -41.059 37.108 8.043   1.00 31.70 ? 203 LYS   A CA   1 
ATOM   1291 C  C    . LYS   A 1 172 ? -41.483 37.327 9.495   1.00 32.01 ? 203 LYS   A C    1 
ATOM   1292 O  O    . LYS   A 1 172 ? -40.767 37.998 10.245  1.00 29.18 ? 203 LYS   A O    1 
ATOM   1293 C  CB   . LYS   A 1 172 ? -41.495 38.277 7.168   1.00 31.89 ? 203 LYS   A CB   1 
ATOM   1294 C  CG   . LYS   A 1 172 ? -40.945 38.154 5.713   1.00 29.21 ? 203 LYS   A CG   1 
ATOM   1295 C  CD   . LYS   A 1 172 ? -39.430 37.856 5.772   1.00 30.13 ? 203 LYS   A CD   1 
ATOM   1296 C  CE   . LYS   A 1 172 ? -38.800 37.865 4.371   1.00 32.24 ? 203 LYS   A CE   1 
ATOM   1297 N  NZ   . LYS   A 1 172 ? -37.323 37.637 4.435   1.00 32.19 ? 203 LYS   A NZ   1 
ATOM   1298 N  N    . ASN   A 1 173 ? -42.642 36.810 9.902   1.00 30.40 ? 204 ASN   A N    1 
ATOM   1299 C  CA   . ASN   A 1 173 ? -43.109 37.035 11.271  1.00 36.50 ? 204 ASN   A CA   1 
ATOM   1300 C  C    . ASN   A 1 173 ? -42.705 35.941 12.249  1.00 29.83 ? 204 ASN   A C    1 
ATOM   1301 O  O    . ASN   A 1 173 ? -42.817 36.152 13.467  1.00 32.07 ? 204 ASN   A O    1 
ATOM   1302 C  CB   . ASN   A 1 173 ? -44.635 37.196 11.291  1.00 35.19 ? 204 ASN   A CB   1 
ATOM   1303 C  CG   . ASN   A 1 173 ? -45.101 38.382 10.450  1.00 41.44 ? 204 ASN   A CG   1 
ATOM   1304 O  OD1  . ASN   A 1 173 ? -44.348 39.338 10.234  1.00 42.38 ? 204 ASN   A OD1  1 
ATOM   1305 N  ND2  . ASN   A 1 173 ? -46.336 38.321 9.965   1.00 39.96 ? 204 ASN   A ND2  1 
ATOM   1306 N  N    . VAL   A 1 174 ? -42.295 34.764 11.769  1.00 30.39 ? 205 VAL   A N    1 
ATOM   1307 C  CA   . VAL   A 1 174 ? -41.967 33.664 12.671  1.00 33.72 ? 205 VAL   A CA   1 
ATOM   1308 C  C    . VAL   A 1 174 ? -40.573 33.105 12.418  1.00 32.15 ? 205 VAL   A C    1 
ATOM   1309 O  O    . VAL   A 1 174 ? -39.657 33.278 13.230  1.00 31.37 ? 205 VAL   A O    1 
ATOM   1310 C  CB   . VAL   A 1 174 ? -43.014 32.536 12.553  1.00 36.21 ? 205 VAL   A CB   1 
ATOM   1311 C  CG1  . VAL   A 1 174 ? -42.748 31.457 13.595  1.00 32.65 ? 205 VAL   A CG1  1 
ATOM   1312 C  CG2  . VAL   A 1 174 ? -44.415 33.091 12.709  1.00 37.79 ? 205 VAL   A CG2  1 
ATOM   1313 N  N    . GLY   A 1 175 ? -40.383 32.462 11.271  1.00 31.27 ? 206 GLY   A N    1 
ATOM   1314 C  CA   . GLY   A 1 175 ? -39.135 31.744 11.049  1.00 31.19 ? 206 GLY   A CA   1 
ATOM   1315 C  C    . GLY   A 1 175 ? -37.914 32.643 10.934  1.00 29.71 ? 206 GLY   A C    1 
ATOM   1316 O  O    . GLY   A 1 175 ? -36.844 32.313 11.446  1.00 30.29 ? 206 GLY   A O    1 
ATOM   1317 N  N    . MET   A 1 176 ? -38.029 33.752 10.197  1.00 36.27 ? 207 MET   A N    1 
ATOM   1318 C  CA   . MET   A 1 176 ? -36.881 34.651 10.053  1.00 33.26 ? 207 MET   A CA   1 
ATOM   1319 C  C    . MET   A 1 176 ? -36.473 35.291 11.377  1.00 33.97 ? 207 MET   A C    1 
ATOM   1320 O  O    . MET   A 1 176 ? -35.270 35.276 11.698  1.00 34.57 ? 207 MET   A O    1 
ATOM   1321 C  CB   . MET   A 1 176 ? -37.176 35.705 8.974   1.00 34.92 ? 207 MET   A CB   1 
ATOM   1322 C  CG   . MET   A 1 176 ? -35.994 36.627 8.644   1.00 35.80 ? 207 MET   A CG   1 
ATOM   1323 S  SD   . MET   A 1 176 ? -35.730 38.008 9.802   1.00 36.39 ? 207 MET   A SD   1 
ATOM   1324 C  CE   . MET   A 1 176 ? -36.935 39.214 9.225   1.00 33.79 ? 207 MET   A CE   1 
ATOM   1325 N  N    . PRO   A 1 177 ? -37.378 35.862 12.183  1.00 31.82 ? 208 PRO   A N    1 
ATOM   1326 C  CA   . PRO   A 1 177 ? -36.937 36.373 13.504  1.00 32.83 ? 208 PRO   A CA   1 
ATOM   1327 C  C    . PRO   A 1 177 ? -36.340 35.308 14.397  1.00 32.29 ? 208 PRO   A C    1 
ATOM   1328 O  O    . PRO   A 1 177 ? -35.418 35.607 15.171  1.00 35.45 ? 208 PRO   A O    1 
ATOM   1329 C  CB   . PRO   A 1 177 ? -38.216 36.959 14.114  1.00 30.91 ? 208 PRO   A CB   1 
ATOM   1330 C  CG   . PRO   A 1 177 ? -39.151 37.164 12.969  1.00 32.23 ? 208 PRO   A CG   1 
ATOM   1331 C  CD   . PRO   A 1 177 ? -38.807 36.124 11.940  1.00 33.44 ? 208 PRO   A CD   1 
ATOM   1332 N  N    . ILE   A 1 178 ? -36.833 34.069 14.335  1.00 33.68 ? 209 ILE   A N    1 
ATOM   1333 C  CA   . ILE   A 1 178 ? -36.272 33.026 15.199  1.00 32.09 ? 209 ILE   A CA   1 
ATOM   1334 C  C    . ILE   A 1 178 ? -34.817 32.764 14.829  1.00 32.13 ? 209 ILE   A C    1 
ATOM   1335 O  O    . ILE   A 1 178 ? -33.937 32.685 15.696  1.00 32.10 ? 209 ILE   A O    1 
ATOM   1336 C  CB   . ILE   A 1 178 ? -37.119 31.741 15.110  1.00 30.79 ? 209 ILE   A CB   1 
ATOM   1337 C  CG1  . ILE   A 1 178 ? -38.446 31.927 15.848  1.00 28.58 ? 209 ILE   A CG1  1 
ATOM   1338 C  CG2  . ILE   A 1 178 ? -36.356 30.556 15.657  1.00 30.67 ? 209 ILE   A CG2  1 
ATOM   1339 C  CD1  . ILE   A 1 178 ? -39.507 30.914 15.415  1.00 33.15 ? 209 ILE   A CD1  1 
ATOM   1340 N  N    . ALA   A 1 179 ? -34.541 32.650 13.520  1.00 34.36 ? 210 ALA   A N    1 
ATOM   1341 C  CA   . ALA   A 1 179 ? -33.168 32.471 13.046  1.00 33.27 ? 210 ALA   A CA   1 
ATOM   1342 C  C    . ALA   A 1 179 ? -32.297 33.671 13.400  1.00 30.96 ? 210 ALA   A C    1 
ATOM   1343 O  O    . ALA   A 1 179 ? -31.128 33.510 13.770  1.00 34.51 ? 210 ALA   A O    1 
ATOM   1344 C  CB   . ALA   A 1 179 ? -33.159 32.225 11.529  1.00 28.15 ? 210 ALA   A CB   1 
ATOM   1345 N  N    . MET   A 1 180 ? -32.842 34.883 13.275  1.00 32.25 ? 211 MET   A N    1 
ATOM   1346 C  CA   . MET   A 1 180 ? -32.084 36.081 13.635  1.00 32.61 ? 211 MET   A CA   1 
ATOM   1347 C  C    . MET   A 1 180 ? -31.709 36.084 15.121  1.00 33.72 ? 211 MET   A C    1 
ATOM   1348 O  O    . MET   A 1 180 ? -30.547 36.300 15.478  1.00 34.40 ? 211 MET   A O    1 
ATOM   1349 C  CB   . MET   A 1 180 ? -32.898 37.327 13.272  1.00 31.41 ? 211 MET   A CB   1 
ATOM   1350 C  CG   . MET   A 1 180 ? -32.144 38.633 13.412  1.00 36.42 ? 211 MET   A CG   1 
ATOM   1351 S  SD   . MET   A 1 180 ? -30.876 38.901 12.131  1.00 37.51 ? 211 MET   A SD   1 
ATOM   1352 C  CE   . MET   A 1 180 ? -31.851 38.866 10.633  1.00 29.36 ? 211 MET   A CE   1 
ATOM   1353 N  N    . LEU   A 1 181 ? -32.677 35.837 16.005  1.00 31.87 ? 212 LEU   A N    1 
ATOM   1354 C  CA   . LEU   A 1 181 ? -32.375 35.823 17.438  1.00 30.00 ? 212 LEU   A CA   1 
ATOM   1355 C  C    . LEU   A 1 181 ? -31.353 34.751 17.779  1.00 31.68 ? 212 LEU   A C    1 
ATOM   1356 O  O    . LEU   A 1 181 ? -30.416 34.996 18.545  1.00 36.46 ? 212 LEU   A O    1 
ATOM   1357 C  CB   . LEU   A 1 181 ? -33.649 35.602 18.252  1.00 26.66 ? 212 LEU   A CB   1 
ATOM   1358 C  CG   . LEU   A 1 181 ? -34.653 36.750 18.198  1.00 30.97 ? 212 LEU   A CG   1 
ATOM   1359 C  CD1  . LEU   A 1 181 ? -35.922 36.361 18.914  1.00 33.16 ? 212 LEU   A CD1  1 
ATOM   1360 C  CD2  . LEU   A 1 181 ? -34.046 38.002 18.809  1.00 33.58 ? 212 LEU   A CD2  1 
ATOM   1361 N  N    . LEU   A 1 182 ? -31.501 33.557 17.221  1.00 32.16 ? 213 LEU   A N    1 
ATOM   1362 C  CA   . LEU   A 1 182 ? -30.655 32.474 17.699  1.00 36.51 ? 213 LEU   A CA   1 
ATOM   1363 C  C    . LEU   A 1 182 ? -29.209 32.573 17.202  1.00 35.83 ? 213 LEU   A C    1 
ATOM   1364 O  O    . LEU   A 1 182 ? -28.303 32.076 17.877  1.00 37.37 ? 213 LEU   A O    1 
ATOM   1365 C  CB   . LEU   A 1 182 ? -31.276 31.126 17.325  1.00 36.71 ? 213 LEU   A CB   1 
ATOM   1366 C  CG   . LEU   A 1 182 ? -32.456 30.784 18.236  1.00 38.41 ? 213 LEU   A CG   1 
ATOM   1367 C  CD1  . LEU   A 1 182 ? -33.142 29.592 17.711  1.00 45.77 ? 213 LEU   A CD1  1 
ATOM   1368 C  CD2  . LEU   A 1 182 ? -31.945 30.499 19.644  1.00 44.01 ? 213 LEU   A CD2  1 
ATOM   1369 N  N    . HIS   A 1 183 ? -28.947 33.217 16.058  1.00 37.35 ? 214 HIS   A N    1 
ATOM   1370 C  CA   . HIS   A 1 183 ? -27.586 33.187 15.520  1.00 35.30 ? 214 HIS   A CA   1 
ATOM   1371 C  C    . HIS   A 1 183 ? -26.754 34.409 15.888  1.00 38.28 ? 214 HIS   A C    1 
ATOM   1372 O  O    . HIS   A 1 183 ? -25.538 34.404 15.656  1.00 40.18 ? 214 HIS   A O    1 
ATOM   1373 C  CB   . HIS   A 1 183 ? -27.603 33.002 13.983  1.00 37.87 ? 214 HIS   A CB   1 
ATOM   1374 C  CG   . HIS   A 1 183 ? -27.633 34.281 13.195  1.00 36.52 ? 214 HIS   A CG   1 
ATOM   1375 N  ND1  . HIS   A 1 183 ? -28.790 34.789 12.644  1.00 37.22 ? 214 HIS   A ND1  1 
ATOM   1376 C  CD2  . HIS   A 1 183 ? -26.638 35.128 12.822  1.00 37.62 ? 214 HIS   A CD2  1 
ATOM   1377 C  CE1  . HIS   A 1 183 ? -28.513 35.905 11.986  1.00 37.00 ? 214 HIS   A CE1  1 
ATOM   1378 N  NE2  . HIS   A 1 183 ? -27.214 36.137 12.087  1.00 32.46 ? 214 HIS   A NE2  1 
ATOM   1379 N  N    . THR   A 1 184 ? -27.352 35.429 16.489  1.00 33.79 ? 215 THR   A N    1 
ATOM   1380 C  CA   . THR   A 1 184 ? -26.677 36.710 16.622  1.00 34.88 ? 215 THR   A CA   1 
ATOM   1381 C  C    . THR   A 1 184 ? -25.922 36.827 17.949  1.00 38.34 ? 215 THR   A C    1 
ATOM   1382 O  O    . THR   A 1 184 ? -26.039 35.993 18.855  1.00 37.49 ? 215 THR   A O    1 
ATOM   1383 C  CB   . THR   A 1 184 ? -27.677 37.850 16.467  1.00 33.78 ? 215 THR   A CB   1 
ATOM   1384 O  OG1  . THR   A 1 184 ? -28.828 37.590 17.286  1.00 34.29 ? 215 THR   A OG1  1 
ATOM   1385 C  CG2  . THR   A 1 184 ? -28.084 37.999 14.974  1.00 34.82 ? 215 THR   A CG2  1 
ATOM   1386 N  N    . ASP   A 1 185 ? -25.140 37.900 18.051  1.00 36.17 ? 216 ASP   A N    1 
ATOM   1387 C  CA   . ASP   A 1 185 ? -24.111 38.000 19.073  1.00 37.36 ? 216 ASP   A CA   1 
ATOM   1388 C  C    . ASP   A 1 185 ? -24.731 38.253 20.445  1.00 36.73 ? 216 ASP   A C    1 
ATOM   1389 O  O    . ASP   A 1 185 ? -25.482 39.213 20.629  1.00 36.74 ? 216 ASP   A O    1 
ATOM   1390 C  CB   . ASP   A 1 185 ? -23.141 39.125 18.706  1.00 36.58 ? 216 ASP   A CB   1 
ATOM   1391 C  CG   . ASP   A 1 185 ? -21.829 39.054 19.476  1.00 41.76 ? 216 ASP   A CG   1 
ATOM   1392 O  OD1  . ASP   A 1 185 ? -21.814 38.553 20.620  1.00 42.50 ? 216 ASP   A OD1  1 
ATOM   1393 O  OD2  . ASP   A 1 185 ? -20.802 39.508 18.932  1.00 45.17 ? 216 ASP   A OD2  1 
ATOM   1394 N  N    . GLY   A 1 186 ? -24.376 37.414 21.419  1.00 36.96 ? 217 GLY   A N    1 
ATOM   1395 C  CA   . GLY   A 1 186 ? -24.801 37.634 22.794  1.00 37.15 ? 217 GLY   A CA   1 
ATOM   1396 C  C    . GLY   A 1 186 ? -24.300 38.934 23.390  1.00 37.44 ? 217 GLY   A C    1 
ATOM   1397 O  O    . GLY   A 1 186 ? -24.833 39.387 24.409  1.00 37.74 ? 217 GLY   A O    1 
ATOM   1398 N  N    . ALA   A 1 187 ? -23.296 39.551 22.776  1.00 39.85 ? 218 ALA   A N    1 
ATOM   1399 C  CA   . ALA   A 1 187 ? -22.700 40.771 23.295  1.00 39.63 ? 218 ALA   A CA   1 
ATOM   1400 C  C    . ALA   A 1 187 ? -23.325 42.037 22.728  1.00 41.80 ? 218 ALA   A C    1 
ATOM   1401 O  O    . ALA   A 1 187 ? -22.920 43.137 23.121  1.00 42.40 ? 218 ALA   A O    1 
ATOM   1402 C  CB   . ALA   A 1 187 ? -21.191 40.780 23.014  1.00 42.62 ? 218 ALA   A CB   1 
ATOM   1403 N  N    . HIS   A 1 188 ? -24.288 41.926 21.815  1.00 38.50 ? 219 HIS   A N    1 
ATOM   1404 C  CA   . HIS   A 1 188 ? -24.877 43.127 21.245  1.00 38.86 ? 219 HIS   A CA   1 
ATOM   1405 C  C    . HIS   A 1 188 ? -25.991 43.660 22.146  1.00 38.91 ? 219 HIS   A C    1 
ATOM   1406 O  O    . HIS   A 1 188 ? -26.390 43.021 23.130  1.00 37.88 ? 219 HIS   A O    1 
ATOM   1407 C  CB   . HIS   A 1 188 ? -25.390 42.849 19.829  1.00 38.74 ? 219 HIS   A CB   1 
ATOM   1408 C  CG   . HIS   A 1 188 ? -24.298 42.688 18.817  1.00 42.38 ? 219 HIS   A CG   1 
ATOM   1409 N  ND1  . HIS   A 1 188 ? -24.522 42.210 17.543  1.00 41.40 ? 219 HIS   A ND1  1 
ATOM   1410 C  CD2  . HIS   A 1 188 ? -22.969 42.942 18.894  1.00 44.54 ? 219 HIS   A CD2  1 
ATOM   1411 C  CE1  . HIS   A 1 188 ? -23.378 42.174 16.881  1.00 42.01 ? 219 HIS   A CE1  1 
ATOM   1412 N  NE2  . HIS   A 1 188 ? -22.420 42.611 17.678  1.00 41.14 ? 219 HIS   A NE2  1 
ATOM   1413 N  N    . GLU   A 1 189 ? -26.471 44.863 21.804  1.00 39.76 ? 220 GLU   A N    1 
ATOM   1414 C  CA   . GLU   A 1 189 ? -27.544 45.545 22.526  1.00 41.43 ? 220 GLU   A CA   1 
ATOM   1415 C  C    . GLU   A 1 189 ? -28.682 44.608 22.897  1.00 42.99 ? 220 GLU   A C    1 
ATOM   1416 O  O    . GLU   A 1 189 ? -29.030 44.460 24.070  1.00 41.32 ? 220 GLU   A O    1 
ATOM   1417 C  CB   . GLU   A 1 189 ? -28.111 46.678 21.674  1.00 43.91 ? 220 GLU   A CB   1 
ATOM   1418 C  CG   . GLU   A 1 189 ? -27.458 48.009 21.831  1.00 50.71 ? 220 GLU   A CG   1 
ATOM   1419 C  CD   . GLU   A 1 189 ? -28.241 49.094 21.120  1.00 55.91 ? 220 GLU   A CD   1 
ATOM   1420 O  OE1  . GLU   A 1 189 ? -29.483 48.939 20.976  1.00 53.14 ? 220 GLU   A OE1  1 
ATOM   1421 O  OE2  . GLU   A 1 189 ? -27.615 50.093 20.695  1.00 58.90 ? 220 GLU   A OE2  1 
ATOM   1422 N  N    . ARG   A 1 190 ? -29.307 44.004 21.888  1.00 38.13 ? 221 ARG   A N    1 
ATOM   1423 C  CA   . ARG   A 1 190 ? -30.252 42.928 22.113  1.00 36.63 ? 221 ARG   A CA   1 
ATOM   1424 C  C    . ARG   A 1 190 ? -29.479 41.639 21.899  1.00 39.24 ? 221 ARG   A C    1 
ATOM   1425 O  O    . ARG   A 1 190 ? -29.127 41.326 20.747  1.00 38.98 ? 221 ARG   A O    1 
ATOM   1426 C  CB   . ARG   A 1 190 ? -31.434 43.027 21.142  1.00 40.37 ? 221 ARG   A CB   1 
ATOM   1427 C  CG   . ARG   A 1 190 ? -32.550 42.005 21.347  1.00 39.64 ? 221 ARG   A CG   1 
ATOM   1428 C  CD   . ARG   A 1 190 ? -32.271 40.687 20.631  1.00 35.86 ? 221 ARG   A CD   1 
ATOM   1429 N  NE   . ARG   A 1 190 ? -32.257 40.865 19.188  1.00 36.89 ? 221 ARG   A NE   1 
ATOM   1430 C  CZ   . ARG   A 1 190 ? -31.408 40.266 18.366  1.00 35.61 ? 221 ARG   A CZ   1 
ATOM   1431 N  NH1  . ARG   A 1 190 ? -31.392 40.541 17.079  1.00 33.93 ? 221 ARG   A NH1  1 
ATOM   1432 N  NH2  . ARG   A 1 190 ? -30.544 39.382 18.852  1.00 37.10 ? 221 ARG   A NH2  1 
ATOM   1433 N  N    . PRO   A 1 191 ? -29.157 40.888 22.955  1.00 34.11 ? 222 PRO   A N    1 
ATOM   1434 C  CA   . PRO   A 1 191 ? -28.336 39.687 22.785  1.00 35.06 ? 222 PRO   A CA   1 
ATOM   1435 C  C    . PRO   A 1 191 ? -29.025 38.665 21.900  1.00 35.14 ? 222 PRO   A C    1 
ATOM   1436 O  O    . PRO   A 1 191 ? -30.250 38.544 21.895  1.00 37.18 ? 222 PRO   A O    1 
ATOM   1437 C  CB   . PRO   A 1 191 ? -28.175 39.152 24.220  1.00 36.55 ? 222 PRO   A CB   1 
ATOM   1438 C  CG   . PRO   A 1 191 ? -28.437 40.338 25.115  1.00 37.65 ? 222 PRO   A CG   1 
ATOM   1439 C  CD   . PRO   A 1 191 ? -29.451 41.174 24.376  1.00 39.96 ? 222 PRO   A CD   1 
ATOM   1440 N  N    . GLY   A 1 192 ? -28.213 37.929 21.138  1.00 39.45 ? 223 GLY   A N    1 
ATOM   1441 C  CA   . GLY   A 1 192 ? -28.657 36.753 20.430  1.00 35.36 ? 223 GLY   A CA   1 
ATOM   1442 C  C    . GLY   A 1 192 ? -28.140 35.478 21.071  1.00 38.46 ? 223 GLY   A C    1 
ATOM   1443 O  O    . GLY   A 1 192 ? -27.505 35.490 22.130  1.00 35.63 ? 223 GLY   A O    1 
ATOM   1444 N  N    . GLY   A 1 193 ? -28.413 34.355 20.393  1.00 34.69 ? 224 GLY   A N    1 
ATOM   1445 C  CA   . GLY   A 1 193 ? -28.085 33.047 20.928  1.00 36.33 ? 224 GLY   A CA   1 
ATOM   1446 C  C    . GLY   A 1 193 ? -26.722 32.493 20.571  1.00 40.88 ? 224 GLY   A C    1 
ATOM   1447 O  O    . GLY   A 1 193 ? -26.303 31.498 21.175  1.00 37.92 ? 224 GLY   A O    1 
ATOM   1448 N  N    . ASP   A 1 194 ? -26.026 33.101 19.597  1.00 38.38 ? 225 ASP   A N    1 
ATOM   1449 C  CA   . ASP   A 1 194 ? -24.684 32.676 19.176  1.00 35.78 ? 225 ASP   A CA   1 
ATOM   1450 C  C    . ASP   A 1 194 ? -24.673 31.239 18.668  1.00 37.21 ? 225 ASP   A C    1 
ATOM   1451 O  O    . ASP   A 1 194 ? -23.659 30.543 18.771  1.00 37.57 ? 225 ASP   A O    1 
ATOM   1452 C  CB   . ASP   A 1 194 ? -23.649 32.839 20.302  1.00 40.60 ? 225 ASP   A CB   1 
ATOM   1453 C  CG   . ASP   A 1 194 ? -23.208 34.284 20.493  1.00 42.21 ? 225 ASP   A CG   1 
ATOM   1454 O  OD1  . ASP   A 1 194 ? -22.823 34.934 19.492  1.00 39.31 ? 225 ASP   A OD1  1 
ATOM   1455 O  OD2  . ASP   A 1 194 ? -23.275 34.779 21.637  1.00 36.89 ? 225 ASP   A OD2  1 
ATOM   1456 N  N    . ALA   A 1 195 ? -25.786 30.783 18.117  1.00 37.00 ? 226 ALA   A N    1 
ATOM   1457 C  CA   . ALA   A 1 195 ? -25.849 29.460 17.515  1.00 38.85 ? 226 ALA   A CA   1 
ATOM   1458 C  C    . ALA   A 1 195 ? -25.507 29.505 16.021  1.00 40.54 ? 226 ALA   A C    1 
ATOM   1459 O  O    . ALA   A 1 195 ? -25.622 30.534 15.351  1.00 40.44 ? 226 ALA   A O    1 
ATOM   1460 C  CB   . ALA   A 1 195 ? -27.237 28.848 17.687  1.00 37.03 ? 226 ALA   A CB   1 
ATOM   1461 N  N    . THR   A 1 196 ? -25.101 28.348 15.508  1.00 39.76 ? 227 THR   A N    1 
ATOM   1462 C  CA   . THR   A 1 196 ? -24.939 28.110 14.082  1.00 39.39 ? 227 THR   A CA   1 
ATOM   1463 C  C    . THR   A 1 196 ? -26.293 27.661 13.559  1.00 42.25 ? 227 THR   A C    1 
ATOM   1464 O  O    . THR   A 1 196 ? -26.777 26.583 13.920  1.00 44.23 ? 227 THR   A O    1 
ATOM   1465 C  CB   . THR   A 1 196 ? -23.870 27.047 13.848  1.00 41.01 ? 227 THR   A CB   1 
ATOM   1466 O  OG1  . THR   A 1 196 ? -22.658 27.455 14.491  1.00 44.33 ? 227 THR   A OG1  1 
ATOM   1467 C  CG2  . THR   A 1 196 ? -23.626 26.822 12.367  1.00 41.10 ? 227 THR   A CG2  1 
ATOM   1468 N  N    . VAL   A 1 197 ? -26.918 28.485 12.728  1.00 36.18 ? 228 VAL   A N    1 
ATOM   1469 C  CA   . VAL   A 1 197 ? -28.328 28.328 12.412  1.00 36.44 ? 228 VAL   A CA   1 
ATOM   1470 C  C    . VAL   A 1 197 ? -28.472 28.004 10.939  1.00 41.47 ? 228 VAL   A C    1 
ATOM   1471 O  O    . VAL   A 1 197 ? -27.955 28.735 10.084  1.00 39.05 ? 228 VAL   A O    1 
ATOM   1472 C  CB   . VAL   A 1 197 ? -29.127 29.590 12.782  1.00 33.23 ? 228 VAL   A CB   1 
ATOM   1473 C  CG1  . VAL   A 1 197 ? -30.535 29.471 12.286  1.00 33.19 ? 228 VAL   A CG1  1 
ATOM   1474 C  CG2  . VAL   A 1 197 ? -29.103 29.800 14.297  1.00 35.35 ? 228 VAL   A CG2  1 
ATOM   1475 N  N    . THR   A 1 198 ? -29.173 26.910 10.646  1.00 37.38 ? 229 THR   A N    1 
ATOM   1476 C  CA   . THR   A 1 198 ? -29.543 26.550 9.284   1.00 40.44 ? 229 THR   A CA   1 
ATOM   1477 C  C    . THR   A 1 198 ? -30.994 26.935 9.053   1.00 38.19 ? 229 THR   A C    1 
ATOM   1478 O  O    . THR   A 1 198 ? -31.879 26.510 9.805   1.00 44.33 ? 229 THR   A O    1 
ATOM   1479 C  CB   . THR   A 1 198 ? -29.358 25.054 9.033   1.00 40.93 ? 229 THR   A CB   1 
ATOM   1480 O  OG1  . THR   A 1 198 ? -27.971 24.719 9.125   1.00 43.74 ? 229 THR   A OG1  1 
ATOM   1481 C  CG2  . THR   A 1 198 ? -29.882 24.688 7.665   1.00 41.28 ? 229 THR   A CG2  1 
ATOM   1482 N  N    . ILE   A 1 199 ? -31.235 27.726 8.017   1.00 38.29 ? 230 ILE   A N    1 
ATOM   1483 C  CA   . ILE   A 1 199 ? -32.577 28.113 7.603   1.00 38.77 ? 230 ILE   A CA   1 
ATOM   1484 C  C    . ILE   A 1 199 ? -32.995 27.201 6.457   1.00 42.61 ? 230 ILE   A C    1 
ATOM   1485 O  O    . ILE   A 1 199 ? -32.342 27.187 5.409   1.00 41.35 ? 230 ILE   A O    1 
ATOM   1486 C  CB   . ILE   A 1 199 ? -32.611 29.589 7.177   1.00 39.61 ? 230 ILE   A CB   1 
ATOM   1487 C  CG1  . ILE   A 1 199 ? -32.155 30.473 8.344   1.00 39.08 ? 230 ILE   A CG1  1 
ATOM   1488 C  CG2  . ILE   A 1 199 ? -34.003 29.988 6.686   1.00 37.82 ? 230 ILE   A CG2  1 
ATOM   1489 C  CD1  . ILE   A 1 199 ? -31.541 31.797 7.905   1.00 41.18 ? 230 ILE   A CD1  1 
ATOM   1490 N  N    . SER   A 1 200 ? -34.074 26.433 6.650   1.00 40.20 ? 231 SER   A N    1 
ATOM   1491 C  CA   . SER   A 1 200 ? -34.659 25.620 5.586   1.00 41.93 ? 231 SER   A CA   1 
ATOM   1492 C  C    . SER   A 1 200 ? -36.077 26.096 5.300   1.00 39.47 ? 231 SER   A C    1 
ATOM   1493 O  O    . SER   A 1 200 ? -36.667 26.855 6.074   1.00 37.70 ? 231 SER   A O    1 
ATOM   1494 C  CB   . SER   A 1 200 ? -34.662 24.129 5.946   1.00 45.37 ? 231 SER   A CB   1 
ATOM   1495 O  OG   . SER   A 1 200 ? -35.326 23.895 7.179   1.00 43.82 ? 231 SER   A OG   1 
ATOM   1496 N  N    . HIS   A 1 201 ? -36.624 25.667 4.172   1.00 38.75 ? 232 HIS   A N    1 
ATOM   1497 C  CA   . HIS   A 1 201 ? -37.888 26.234 3.713   1.00 38.10 ? 232 HIS   A CA   1 
ATOM   1498 C  C    . HIS   A 1 201 ? -38.522 25.278 2.708   1.00 37.12 ? 232 HIS   A C    1 
ATOM   1499 O  O    . HIS   A 1 201 ? -38.095 24.129 2.568   1.00 41.34 ? 232 HIS   A O    1 
ATOM   1500 C  CB   . HIS   A 1 201 ? -37.668 27.636 3.144   1.00 36.09 ? 232 HIS   A CB   1 
ATOM   1501 C  CG   . HIS   A 1 201 ? -36.512 27.717 2.199   1.00 41.54 ? 232 HIS   A CG   1 
ATOM   1502 N  ND1  . HIS   A 1 201 ? -36.584 27.260 0.898   1.00 39.60 ? 232 HIS   A ND1  1 
ATOM   1503 C  CD2  . HIS   A 1 201 ? -35.246 28.167 2.372   1.00 38.47 ? 232 HIS   A CD2  1 
ATOM   1504 C  CE1  . HIS   A 1 201 ? -35.415 27.443 0.308   1.00 39.96 ? 232 HIS   A CE1  1 
ATOM   1505 N  NE2  . HIS   A 1 201 ? -34.587 27.993 1.178   1.00 39.51 ? 232 HIS   A NE2  1 
ATOM   1506 N  N    . ARG   A 1 202 ? -39.566 25.753 2.024   1.00 36.91 ? 233 ARG   A N    1 
ATOM   1507 C  CA   . ARG   A 1 202 ? -40.338 24.908 1.119   1.00 41.00 ? 233 ARG   A CA   1 
ATOM   1508 C  C    . ARG   A 1 202 ? -39.515 24.338 -0.035  1.00 44.37 ? 233 ARG   A C    1 
ATOM   1509 O  O    . ARG   A 1 202 ? -39.950 23.356 -0.653  1.00 45.85 ? 233 ARG   A O    1 
ATOM   1510 C  CB   . ARG   A 1 202 ? -41.506 25.698 0.542   1.00 41.25 ? 233 ARG   A CB   1 
ATOM   1511 C  CG   . ARG   A 1 202 ? -41.064 26.755 -0.467  1.00 41.66 ? 233 ARG   A CG   1 
ATOM   1512 C  CD   . ARG   A 1 202 ? -42.252 27.526 -1.003  1.00 42.77 ? 233 ARG   A CD   1 
ATOM   1513 N  NE   . ARG   A 1 202 ? -42.943 28.265 0.045   1.00 41.58 ? 233 ARG   A NE   1 
ATOM   1514 C  CZ   . ARG   A 1 202 ? -44.091 27.899 0.606   1.00 46.46 ? 233 ARG   A CZ   1 
ATOM   1515 N  NH1  . ARG   A 1 202 ? -44.734 28.697 1.449   1.00 42.63 ? 233 ARG   A NH1  1 
ATOM   1516 N  NH2  . ARG   A 1 202 ? -44.610 26.707 0.315   1.00 44.59 ? 233 ARG   A NH2  1 
ATOM   1517 N  N    . TYR   A 1 203 ? -38.356 24.920 -0.362  1.00 41.73 ? 234 TYR   A N    1 
ATOM   1518 C  CA   . TYR   A 1 203 ? -37.532 24.396 -1.450  1.00 42.47 ? 234 TYR   A CA   1 
ATOM   1519 C  C    . TYR   A 1 203 ? -36.360 23.579 -0.957  1.00 45.10 ? 234 TYR   A C    1 
ATOM   1520 O  O    . TYR   A 1 203 ? -35.574 23.101 -1.773  1.00 44.53 ? 234 TYR   A O    1 
ATOM   1521 C  CB   . TYR   A 1 203 ? -37.043 25.531 -2.365  1.00 43.24 ? 234 TYR   A CB   1 
ATOM   1522 C  CG   . TYR   A 1 203 ? -38.212 26.212 -3.021  1.00 40.79 ? 234 TYR   A CG   1 
ATOM   1523 C  CD1  . TYR   A 1 203 ? -39.166 25.469 -3.710  1.00 44.75 ? 234 TYR   A CD1  1 
ATOM   1524 C  CD2  . TYR   A 1 203 ? -38.416 27.573 -2.884  1.00 38.89 ? 234 TYR   A CD2  1 
ATOM   1525 C  CE1  . TYR   A 1 203 ? -40.265 26.076 -4.282  1.00 44.37 ? 234 TYR   A CE1  1 
ATOM   1526 C  CE2  . TYR   A 1 203 ? -39.517 28.184 -3.435  1.00 38.28 ? 234 TYR   A CE2  1 
ATOM   1527 C  CZ   . TYR   A 1 203 ? -40.435 27.434 -4.139  1.00 43.80 ? 234 TYR   A CZ   1 
ATOM   1528 O  OH   . TYR   A 1 203 ? -41.527 28.049 -4.701  1.00 43.21 ? 234 TYR   A OH   1 
ATOM   1529 N  N    . THR   A 1 204 ? -36.227 23.402 0.350   1.00 42.70 ? 235 THR   A N    1 
ATOM   1530 C  CA   . THR   A 1 204 ? -35.233 22.483 0.889   1.00 45.95 ? 235 THR   A CA   1 
ATOM   1531 C  C    . THR   A 1 204 ? -35.709 21.055 0.649   1.00 48.19 ? 235 THR   A C    1 
ATOM   1532 O  O    . THR   A 1 204 ? -36.804 20.695 1.111   1.00 47.97 ? 235 THR   A O    1 
ATOM   1533 C  CB   . THR   A 1 204 ? -35.035 22.726 2.396   1.00 46.56 ? 235 THR   A CB   1 
ATOM   1534 O  OG1  . THR   A 1 204 ? -34.716 24.107 2.630   1.00 43.32 ? 235 THR   A OG1  1 
ATOM   1535 C  CG2  . THR   A 1 204 ? -33.922 21.847 2.937   1.00 45.64 ? 235 THR   A CG2  1 
ATOM   1536 N  N    . PRO   A 1 205 ? -34.953 20.218 -0.062  1.00 52.23 ? 236 PRO   A N    1 
ATOM   1537 C  CA   . PRO   A 1 205 ? -35.398 18.831 -0.261  1.00 52.63 ? 236 PRO   A CA   1 
ATOM   1538 C  C    . PRO   A 1 205 ? -35.403 18.078 1.060   1.00 52.24 ? 236 PRO   A C    1 
ATOM   1539 O  O    . PRO   A 1 205 ? -34.514 18.260 1.899   1.00 51.12 ? 236 PRO   A O    1 
ATOM   1540 C  CB   . PRO   A 1 205 ? -34.362 18.254 -1.237  1.00 48.90 ? 236 PRO   A CB   1 
ATOM   1541 C  CG   . PRO   A 1 205 ? -33.676 19.465 -1.852  1.00 53.11 ? 236 PRO   A CG   1 
ATOM   1542 C  CD   . PRO   A 1 205 ? -33.664 20.478 -0.730  1.00 50.93 ? 236 PRO   A CD   1 
ATOM   1543 N  N    . LYS   A 1 206 ? -36.400 17.200 1.218   1.00 50.54 ? 237 LYS   A N    1 
ATOM   1544 C  CA   . LYS   A 1 206 ? -36.557 16.461 2.467   1.00 50.49 ? 237 LYS   A CA   1 
ATOM   1545 C  C    . LYS   A 1 206 ? -35.256 15.788 2.879   1.00 53.36 ? 237 LYS   A C    1 
ATOM   1546 O  O    . LYS   A 1 206 ? -34.916 15.741 4.068   1.00 55.52 ? 237 LYS   A O    1 
ATOM   1547 C  CB   . LYS   A 1 206 ? -37.673 15.423 2.325   1.00 55.77 ? 237 LYS   A CB   1 
ATOM   1548 C  CG   . LYS   A 1 206 ? -37.857 14.535 3.551   1.00 59.68 ? 237 LYS   A CG   1 
ATOM   1549 C  CD   . LYS   A 1 206 ? -38.798 13.350 3.290   1.00 68.23 ? 237 LYS   A CD   1 
ATOM   1550 C  CE   . LYS   A 1 206 ? -38.081 12.183 2.606   1.00 76.50 ? 237 LYS   A CE   1 
ATOM   1551 N  NZ   . LYS   A 1 206 ? -38.936 10.957 2.496   1.00 81.10 ? 237 LYS   A NZ   1 
ATOM   1552 N  N    . GLU   A 1 207 ? -34.504 15.273 1.906   1.00 53.63 ? 238 GLU   A N    1 
ATOM   1553 C  CA   . GLU   A 1 207 ? -33.240 14.616 2.215   1.00 52.77 ? 238 GLU   A CA   1 
ATOM   1554 C  C    . GLU   A 1 207 ? -32.230 15.592 2.802   1.00 53.12 ? 238 GLU   A C    1 
ATOM   1555 O  O    . GLU   A 1 207 ? -31.468 15.238 3.710   1.00 55.54 ? 238 GLU   A O    1 
ATOM   1556 C  CB   . GLU   A 1 207 ? -32.680 13.961 0.955   1.00 60.79 ? 238 GLU   A CB   1 
ATOM   1557 C  CG   . GLU   A 1 207 ? -31.342 13.280 1.149   1.00 65.67 ? 238 GLU   A CG   1 
ATOM   1558 C  CD   . GLU   A 1 207 ? -30.989 12.378 -0.023  1.00 82.56 ? 238 GLU   A CD   1 
ATOM   1559 O  OE1  . GLU   A 1 207 ? -30.318 12.860 -0.969  1.00 83.42 ? 238 GLU   A OE1  1 
ATOM   1560 O  OE2  . GLU   A 1 207 ? -31.400 11.193 -0.009  1.00 90.78 ? 238 GLU   A OE2  1 
ATOM   1561 N  N    . GLN   A 1 208 ? -32.190 16.822 2.279   1.00 55.54 ? 239 GLN   A N    1 
ATOM   1562 C  CA   . GLN   A 1 208 ? -31.220 17.802 2.764   1.00 53.49 ? 239 GLN   A CA   1 
ATOM   1563 C  C    . GLN   A 1 208 ? -31.617 18.346 4.133   1.00 49.96 ? 239 GLN   A C    1 
ATOM   1564 O  O    . GLN   A 1 208 ? -30.753 18.594 4.986   1.00 50.11 ? 239 GLN   A O    1 
ATOM   1565 C  CB   . GLN   A 1 208 ? -31.073 18.935 1.743   1.00 51.91 ? 239 GLN   A CB   1 
ATOM   1566 C  CG   . GLN   A 1 208 ? -30.662 18.460 0.351   1.00 52.73 ? 239 GLN   A CG   1 
ATOM   1567 C  CD   . GLN   A 1 208 ? -29.291 17.806 0.335   1.00 53.56 ? 239 GLN   A CD   1 
ATOM   1568 O  OE1  . GLN   A 1 208 ? -28.402 18.184 1.092   1.00 54.49 ? 239 GLN   A OE1  1 
ATOM   1569 N  NE2  . GLN   A 1 208 ? -29.117 16.815 -0.529  1.00 63.25 ? 239 GLN   A NE2  1 
ATOM   1570 N  N    . LEU   A 1 209 ? -32.918 18.536 4.364   1.00 51.50 ? 240 LEU   A N    1 
ATOM   1571 C  CA   . LEU   A 1 209 ? -33.379 18.907 5.702   1.00 50.87 ? 240 LEU   A CA   1 
ATOM   1572 C  C    . LEU   A 1 209 ? -32.880 17.910 6.739   1.00 49.47 ? 240 LEU   A C    1 
ATOM   1573 O  O    . LEU   A 1 209 ? -32.243 18.289 7.730   1.00 52.45 ? 240 LEU   A O    1 
ATOM   1574 C  CB   . LEU   A 1 209 ? -34.904 18.996 5.723   1.00 51.45 ? 240 LEU   A CB   1 
ATOM   1575 C  CG   . LEU   A 1 209 ? -35.512 19.202 7.112   1.00 53.41 ? 240 LEU   A CG   1 
ATOM   1576 C  CD1  . LEU   A 1 209 ? -35.031 20.523 7.707   1.00 49.40 ? 240 LEU   A CD1  1 
ATOM   1577 C  CD2  . LEU   A 1 209 ? -37.029 19.154 7.039   1.00 48.30 ? 240 LEU   A CD2  1 
ATOM   1578 N  N    . LYS   A 1 210 ? -33.111 16.617 6.489   1.00 50.79 ? 241 LYS   A N    1 
ATOM   1579 C  CA   . LYS   A 1 210 ? -32.658 15.573 7.405   1.00 52.26 ? 241 LYS   A CA   1 
ATOM   1580 C  C    . LYS   A 1 210 ? -31.146 15.617 7.619   1.00 51.38 ? 241 LYS   A C    1 
ATOM   1581 O  O    . LYS   A 1 210 ? -30.664 15.374 8.730   1.00 51.54 ? 241 LYS   A O    1 
ATOM   1582 C  CB   . LYS   A 1 210 ? -33.083 14.197 6.877   1.00 56.44 ? 241 LYS   A CB   1 
ATOM   1583 C  CG   . LYS   A 1 210 ? -32.456 13.012 7.621   1.00 59.19 ? 241 LYS   A CG   1 
ATOM   1584 C  CD   . LYS   A 1 210 ? -33.038 11.684 7.154   1.00 59.00 ? 241 LYS   A CD   1 
ATOM   1585 C  CE   . LYS   A 1 210 ? -32.576 10.521 8.031   1.00 64.44 ? 241 LYS   A CE   1 
ATOM   1586 N  NZ   . LYS   A 1 210 ? -33.308 9.269  7.683   1.00 59.66 ? 241 LYS   A NZ   1 
ATOM   1587 N  N    . LYS   A 1 211 ? -30.376 15.907 6.566   1.00 54.72 ? 242 LYS   A N    1 
ATOM   1588 C  CA   . LYS   A 1 211 ? -28.921 15.941 6.701   1.00 53.53 ? 242 LYS   A CA   1 
ATOM   1589 C  C    . LYS   A 1 211 ? -28.445 17.114 7.553   1.00 52.39 ? 242 LYS   A C    1 
ATOM   1590 O  O    . LYS   A 1 211 ? -27.319 17.080 8.064   1.00 53.50 ? 242 LYS   A O    1 
ATOM   1591 C  CB   . LYS   A 1 211 ? -28.269 15.963 5.312   1.00 55.17 ? 242 LYS   A CB   1 
ATOM   1592 C  CG   . LYS   A 1 211 ? -28.489 14.658 4.538   1.00 57.80 ? 242 LYS   A CG   1 
ATOM   1593 C  CD   . LYS   A 1 211 ? -28.209 14.788 3.039   1.00 65.83 ? 242 LYS   A CD   1 
ATOM   1594 C  CE   . LYS   A 1 211 ? -26.709 14.844 2.693   1.00 71.60 ? 242 LYS   A CE   1 
ATOM   1595 N  NZ   . LYS   A 1 211 ? -25.934 13.603 3.028   1.00 79.45 ? 242 LYS   A NZ   1 
ATOM   1596 N  N    . HIS   A 1 212 ? -29.277 18.138 7.738   1.00 46.92 ? 243 HIS   A N    1 
ATOM   1597 C  CA   . HIS   A 1 212 ? -28.927 19.215 8.655   1.00 50.16 ? 243 HIS   A CA   1 
ATOM   1598 C  C    . HIS   A 1 212 ? -29.489 18.987 10.065  1.00 44.59 ? 243 HIS   A C    1 
ATOM   1599 O  O    . HIS   A 1 212 ? -28.768 19.161 11.051  1.00 47.17 ? 243 HIS   A O    1 
ATOM   1600 C  CB   . HIS   A 1 212 ? -29.409 20.547 8.075   1.00 43.92 ? 243 HIS   A CB   1 
ATOM   1601 C  CG   . HIS   A 1 212 ? -28.624 21.004 6.876   1.00 52.20 ? 243 HIS   A CG   1 
ATOM   1602 N  ND1  . HIS   A 1 212 ? -29.079 20.854 5.583   1.00 50.98 ? 243 HIS   A ND1  1 
ATOM   1603 C  CD2  . HIS   A 1 212 ? -27.414 21.606 6.779   1.00 48.41 ? 243 HIS   A CD2  1 
ATOM   1604 C  CE1  . HIS   A 1 212 ? -28.187 21.349 4.743   1.00 50.93 ? 243 HIS   A CE1  1 
ATOM   1605 N  NE2  . HIS   A 1 212 ? -27.167 21.810 5.444   1.00 54.30 ? 243 HIS   A NE2  1 
ATOM   1606 N  N    . THR   A 1 213 ? -30.758 18.579 10.180  1.00 47.01 ? 244 THR   A N    1 
ATOM   1607 C  CA   . THR   A 1 213 ? -31.349 18.353 11.499  1.00 46.45 ? 244 THR   A CA   1 
ATOM   1608 C  C    . THR   A 1 213 ? -30.582 17.295 12.280  1.00 48.49 ? 244 THR   A C    1 
ATOM   1609 O  O    . THR   A 1 213 ? -30.454 17.389 13.507  1.00 48.19 ? 244 THR   A O    1 
ATOM   1610 C  CB   . THR   A 1 213 ? -32.818 17.944 11.372  1.00 48.93 ? 244 THR   A CB   1 
ATOM   1611 O  OG1  . THR   A 1 213 ? -32.934 16.815 10.497  1.00 53.25 ? 244 THR   A OG1  1 
ATOM   1612 C  CG2  . THR   A 1 213 ? -33.677 19.103 10.853  1.00 43.47 ? 244 THR   A CG2  1 
ATOM   1613 N  N    . ILE   A 1 214 ? -30.051 16.286 11.586  1.00 50.09 ? 245 ILE   A N    1 
ATOM   1614 C  CA   . ILE   A 1 214 ? -29.347 15.201 12.260  1.00 53.15 ? 245 ILE   A CA   1 
ATOM   1615 C  C    . ILE   A 1 214 ? -28.077 15.693 12.958  1.00 51.60 ? 245 ILE   A C    1 
ATOM   1616 O  O    . ILE   A 1 214 ? -27.591 15.039 13.886  1.00 54.98 ? 245 ILE   A O    1 
ATOM   1617 C  CB   . ILE   A 1 214 ? -29.066 14.053 11.255  1.00 55.09 ? 245 ILE   A CB   1 
ATOM   1618 C  CG1  . ILE   A 1 214 ? -28.793 12.746 12.002  1.00 57.78 ? 245 ILE   A CG1  1 
ATOM   1619 C  CG2  . ILE   A 1 214 ? -27.915 14.401 10.306  1.00 52.83 ? 245 ILE   A CG2  1 
ATOM   1620 C  CD1  . ILE   A 1 214 ? -30.037 12.126 12.615  1.00 60.78 ? 245 ILE   A CD1  1 
ATOM   1621 N  N    . LEU   A 1 215 ? -27.539 16.844 12.555  1.00 49.88 ? 246 LEU   A N    1 
ATOM   1622 C  CA   . LEU   A 1 215 ? -26.431 17.477 13.266  1.00 50.00 ? 246 LEU   A CA   1 
ATOM   1623 C  C    . LEU   A 1 215 ? -26.885 18.405 14.384  1.00 48.65 ? 246 LEU   A C    1 
ATOM   1624 O  O    . LEU   A 1 215 ? -26.039 18.912 15.128  1.00 47.27 ? 246 LEU   A O    1 
ATOM   1625 C  CB   . LEU   A 1 215 ? -25.576 18.302 12.300  1.00 51.30 ? 246 LEU   A CB   1 
ATOM   1626 C  CG   . LEU   A 1 215 ? -25.028 17.628 11.045  1.00 55.16 ? 246 LEU   A CG   1 
ATOM   1627 C  CD1  . LEU   A 1 215 ? -24.670 18.687 10.022  1.00 54.75 ? 246 LEU   A CD1  1 
ATOM   1628 C  CD2  . LEU   A 1 215 ? -23.809 16.799 11.403  1.00 53.67 ? 246 LEU   A CD2  1 
ATOM   1629 N  N    . ALA   A 1 216 ? -28.184 18.653 14.504  1.00 48.79 ? 247 ALA   A N    1 
ATOM   1630 C  CA   . ALA   A 1 216 ? -28.686 19.795 15.255  1.00 49.66 ? 247 ALA   A CA   1 
ATOM   1631 C  C    . ALA   A 1 216 ? -28.870 19.478 16.736  1.00 49.18 ? 247 ALA   A C    1 
ATOM   1632 O  O    . ALA   A 1 216 ? -29.373 18.414 17.104  1.00 49.81 ? 247 ALA   A O    1 
ATOM   1633 C  CB   . ALA   A 1 216 ? -30.014 20.272 14.661  1.00 42.83 ? 247 ALA   A CB   1 
ATOM   1634 N  N    . ASP   A 1 217 ? -28.468 20.426 17.582  1.00 47.52 ? 248 ASP   A N    1 
ATOM   1635 C  CA   . ASP   A 1 217 ? -28.812 20.388 18.997  1.00 48.06 ? 248 ASP   A CA   1 
ATOM   1636 C  C    . ASP   A 1 217 ? -30.193 20.959 19.285  1.00 49.34 ? 248 ASP   A C    1 
ATOM   1637 O  O    . ASP   A 1 217 ? -30.785 20.625 20.322  1.00 44.83 ? 248 ASP   A O    1 
ATOM   1638 C  CB   . ASP   A 1 217 ? -27.774 21.153 19.806  1.00 45.33 ? 248 ASP   A CB   1 
ATOM   1639 C  CG   . ASP   A 1 217 ? -26.366 20.685 19.518  1.00 52.88 ? 248 ASP   A CG   1 
ATOM   1640 O  OD1  . ASP   A 1 217 ? -25.678 21.344 18.710  1.00 50.70 ? 248 ASP   A OD1  1 
ATOM   1641 O  OD2  . ASP   A 1 217 ? -25.953 19.650 20.088  1.00 56.28 ? 248 ASP   A OD2  1 
ATOM   1642 N  N    . ILE   A 1 218 ? -30.705 21.832 18.416  1.00 43.65 ? 249 ILE   A N    1 
ATOM   1643 C  CA   . ILE   A 1 218 ? -32.056 22.374 18.539  1.00 39.73 ? 249 ILE   A CA   1 
ATOM   1644 C  C    . ILE   A 1 218 ? -32.690 22.389 17.157  1.00 43.72 ? 249 ILE   A C    1 
ATOM   1645 O  O    . ILE   A 1 218 ? -32.095 22.900 16.198  1.00 39.94 ? 249 ILE   A O    1 
ATOM   1646 C  CB   . ILE   A 1 218 ? -32.066 23.795 19.138  1.00 40.58 ? 249 ILE   A CB   1 
ATOM   1647 C  CG1  . ILE   A 1 218 ? -31.176 23.880 20.390  1.00 43.64 ? 249 ILE   A CG1  1 
ATOM   1648 C  CG2  . ILE   A 1 218 ? -33.495 24.224 19.426  1.00 39.48 ? 249 ILE   A CG2  1 
ATOM   1649 C  CD1  . ILE   A 1 218 ? -31.151 25.255 21.055  1.00 37.50 ? 249 ILE   A CD1  1 
ATOM   1650 N  N    . VAL   A 1 219 ? -33.891 21.829 17.050  1.00 37.70 ? 250 VAL   A N    1 
ATOM   1651 C  CA   . VAL   A 1 219 ? -34.669 21.871 15.818  1.00 41.23 ? 250 VAL   A CA   1 
ATOM   1652 C  C    . VAL   A 1 219 ? -35.945 22.637 16.109  1.00 40.78 ? 250 VAL   A C    1 
ATOM   1653 O  O    . VAL   A 1 219 ? -36.644 22.337 17.086  1.00 42.53 ? 250 VAL   A O    1 
ATOM   1654 C  CB   . VAL   A 1 219 ? -34.979 20.465 15.280  1.00 39.50 ? 250 VAL   A CB   1 
ATOM   1655 C  CG1  . VAL   A 1 219 ? -35.836 20.565 14.062  1.00 39.93 ? 250 VAL   A CG1  1 
ATOM   1656 C  CG2  . VAL   A 1 219 ? -33.691 19.735 14.972  1.00 42.30 ? 250 VAL   A CG2  1 
ATOM   1657 N  N    . ILE   A 1 220 ? -36.218 23.659 15.305  1.00 35.17 ? 251 ILE   A N    1 
ATOM   1658 C  CA   . ILE   A 1 220 ? -37.366 24.533 15.504  1.00 35.08 ? 251 ILE   A CA   1 
ATOM   1659 C  C    . ILE   A 1 220 ? -38.172 24.517 14.222  1.00 40.27 ? 251 ILE   A C    1 
ATOM   1660 O  O    . ILE   A 1 220 ? -37.723 25.036 13.187  1.00 41.02 ? 251 ILE   A O    1 
ATOM   1661 C  CB   . ILE   A 1 220 ? -36.937 25.955 15.874  1.00 40.39 ? 251 ILE   A CB   1 
ATOM   1662 C  CG1  . ILE   A 1 220 ? -36.020 25.893 17.088  1.00 38.42 ? 251 ILE   A CG1  1 
ATOM   1663 C  CG2  . ILE   A 1 220 ? -38.164 26.859 16.134  1.00 39.43 ? 251 ILE   A CG2  1 
ATOM   1664 C  CD1  . ILE   A 1 220 ? -35.505 27.207 17.504  1.00 38.96 ? 251 ILE   A CD1  1 
ATOM   1665 N  N    . SER   A 1 221 ? -39.366 23.938 14.277  1.00 38.93 ? 252 SER   A N    1 
ATOM   1666 C  CA   . SER   A 1 221 ? -40.159 23.739 13.073  1.00 44.30 ? 252 SER   A CA   1 
ATOM   1667 C  C    . SER   A 1 221 ? -41.306 24.730 13.079  1.00 43.20 ? 252 SER   A C    1 
ATOM   1668 O  O    . SER   A 1 221 ? -42.142 24.714 13.990  1.00 36.15 ? 252 SER   A O    1 
ATOM   1669 C  CB   . SER   A 1 221 ? -40.678 22.306 12.962  1.00 46.77 ? 252 SER   A CB   1 
ATOM   1670 O  OG   . SER   A 1 221 ? -41.316 22.126 11.712  1.00 45.49 ? 252 SER   A OG   1 
ATOM   1671 N  N    . ALA   A 1 222 ? -41.331 25.592 12.065  1.00 39.46 ? 253 ALA   A N    1 
ATOM   1672 C  CA   . ALA   A 1 222 ? -42.366 26.593 11.866  1.00 37.75 ? 253 ALA   A CA   1 
ATOM   1673 C  C    . ALA   A 1 222 ? -42.834 26.561 10.420  1.00 42.77 ? 253 ALA   A C    1 
ATOM   1674 O  O    . ALA   A 1 222 ? -42.928 27.589 9.743   1.00 38.75 ? 253 ALA   A O    1 
ATOM   1675 C  CB   . ALA   A 1 222 ? -41.871 27.984 12.251  1.00 34.68 ? 253 ALA   A CB   1 
ATOM   1676 N  N    . ALA   A 1 223 ? -43.131 25.358 9.924   1.00 41.81 ? 254 ALA   A N    1 
ATOM   1677 C  CA   . ALA   A 1 223 ? -43.533 25.176 8.529   1.00 42.59 ? 254 ALA   A CA   1 
ATOM   1678 C  C    . ALA   A 1 223 ? -45.025 24.937 8.344   1.00 44.88 ? 254 ALA   A C    1 
ATOM   1679 O  O    . ALA   A 1 223 ? -45.577 25.311 7.306   1.00 45.64 ? 254 ALA   A O    1 
ATOM   1680 C  CB   . ALA   A 1 223 ? -42.768 24.003 7.910   1.00 42.52 ? 254 ALA   A CB   1 
ATOM   1681 N  N    . GLY   A 1 224 ? -45.699 24.330 9.312   1.00 45.67 ? 255 GLY   A N    1 
ATOM   1682 C  CA   . GLY   A 1 224 ? -47.104 24.027 9.124   1.00 44.69 ? 255 GLY   A CA   1 
ATOM   1683 C  C    . GLY   A 1 224 ? -47.339 22.782 8.300   1.00 46.76 ? 255 GLY   A C    1 
ATOM   1684 O  O    . GLY   A 1 224 ? -48.231 22.768 7.440   1.00 45.64 ? 255 GLY   A O    1 
ATOM   1685 N  N    . ILE   A 1 225 ? -46.554 21.730 8.540   1.00 48.24 ? 256 ILE   A N    1 
ATOM   1686 C  CA   . ILE   A 1 225 ? -46.667 20.476 7.814   1.00 50.70 ? 256 ILE   A CA   1 
ATOM   1687 C  C    . ILE   A 1 225 ? -46.637 19.346 8.837   1.00 50.38 ? 256 ILE   A C    1 
ATOM   1688 O  O    . ILE   A 1 225 ? -45.619 19.153 9.508   1.00 48.18 ? 256 ILE   A O    1 
ATOM   1689 C  CB   . ILE   A 1 225 ? -45.546 20.284 6.780   1.00 49.90 ? 256 ILE   A CB   1 
ATOM   1690 C  CG1  . ILE   A 1 225 ? -45.848 21.093 5.523   1.00 52.82 ? 256 ILE   A CG1  1 
ATOM   1691 C  CG2  . ILE   A 1 225 ? -45.373 18.808 6.447   1.00 52.82 ? 256 ILE   A CG2  1 
ATOM   1692 C  CD1  . ILE   A 1 225 ? -44.619 21.661 4.895   1.00 50.76 ? 256 ILE   A CD1  1 
ATOM   1693 N  N    . PRO   A 1 226 ? -47.718 18.583 8.990   1.00 52.32 ? 257 PRO   A N    1 
ATOM   1694 C  CA   . PRO   A 1 226 ? -47.706 17.466 9.939   1.00 51.04 ? 257 PRO   A CA   1 
ATOM   1695 C  C    . PRO   A 1 226 ? -46.614 16.462 9.611   1.00 51.36 ? 257 PRO   A C    1 
ATOM   1696 O  O    . PRO   A 1 226 ? -46.336 16.172 8.444   1.00 49.88 ? 257 PRO   A O    1 
ATOM   1697 C  CB   . PRO   A 1 226 ? -49.102 16.856 9.774   1.00 51.34 ? 257 PRO   A CB   1 
ATOM   1698 C  CG   . PRO   A 1 226 ? -49.945 18.003 9.349   1.00 52.43 ? 257 PRO   A CG   1 
ATOM   1699 C  CD   . PRO   A 1 226 ? -49.061 18.817 8.437   1.00 51.57 ? 257 PRO   A CD   1 
ATOM   1700 N  N    . ASN   A 1 227 ? -45.978 15.954 10.665  1.00 50.00 ? 258 ASN   A N    1 
ATOM   1701 C  CA   . ASN   A 1 227 ? -44.929 14.936 10.569  1.00 52.78 ? 258 ASN   A CA   1 
ATOM   1702 C  C    . ASN   A 1 227 ? -43.769 15.382 9.683   1.00 53.17 ? 258 ASN   A C    1 
ATOM   1703 O  O    . ASN   A 1 227 ? -43.123 14.564 9.023   1.00 52.48 ? 258 ASN   A O    1 
ATOM   1704 C  CB   . ASN   A 1 227 ? -45.493 13.600 10.076  1.00 51.63 ? 258 ASN   A CB   1 
ATOM   1705 C  CG   . ASN   A 1 227 ? -46.564 13.047 10.994  1.00 56.92 ? 258 ASN   A CG   1 
ATOM   1706 O  OD1  . ASN   A 1 227 ? -46.292 12.700 12.145  1.00 52.01 ? 258 ASN   A OD1  1 
ATOM   1707 N  ND2  . ASN   A 1 227 ? -47.789 12.958 10.486  1.00 52.90 ? 258 ASN   A ND2  1 
ATOM   1708 N  N    . LEU   A 1 228 ? -43.480 16.683 9.666   1.00 52.71 ? 259 LEU   A N    1 
ATOM   1709 C  CA   . LEU   A 1 228 ? -42.281 17.144 8.975   1.00 49.59 ? 259 LEU   A CA   1 
ATOM   1710 C  C    . LEU   A 1 228 ? -41.023 16.639 9.674   1.00 51.45 ? 259 LEU   A C    1 
ATOM   1711 O  O    . LEU   A 1 228 ? -40.024 16.310 9.022   1.00 49.33 ? 259 LEU   A O    1 
ATOM   1712 C  CB   . LEU   A 1 228 ? -42.284 18.667 8.898   1.00 48.69 ? 259 LEU   A CB   1 
ATOM   1713 C  CG   . LEU   A 1 228 ? -41.133 19.277 8.105   1.00 48.07 ? 259 LEU   A CG   1 
ATOM   1714 C  CD1  . LEU   A 1 228 ? -41.328 18.984 6.604   1.00 46.79 ? 259 LEU   A CD1  1 
ATOM   1715 C  CD2  . LEU   A 1 228 ? -41.013 20.774 8.375   1.00 45.04 ? 259 LEU   A CD2  1 
ATOM   1716 N  N    . ILE   A 1 229 ? -41.059 16.556 10.999  1.00 48.35 ? 260 ILE   A N    1 
ATOM   1717 C  CA   . ILE   A 1 229 ? -39.904 16.190 11.807  1.00 50.60 ? 260 ILE   A CA   1 
ATOM   1718 C  C    . ILE   A 1 229 ? -40.190 14.836 12.444  1.00 55.15 ? 260 ILE   A C    1 
ATOM   1719 O  O    . ILE   A 1 229 ? -41.165 14.689 13.192  1.00 56.28 ? 260 ILE   A O    1 
ATOM   1720 C  CB   . ILE   A 1 229 ? -39.614 17.261 12.868  1.00 49.18 ? 260 ILE   A CB   1 
ATOM   1721 C  CG1  . ILE   A 1 229 ? -39.544 18.637 12.204  1.00 46.50 ? 260 ILE   A CG1  1 
ATOM   1722 C  CG2  . ILE   A 1 229 ? -38.326 16.961 13.600  1.00 49.07 ? 260 ILE   A CG2  1 
ATOM   1723 C  CD1  . ILE   A 1 229 ? -38.317 18.830 11.340  1.00 45.22 ? 260 ILE   A CD1  1 
ATOM   1724 N  N    . THR   A 1 230 ? -39.337 13.852 12.157  1.00 57.30 ? 261 THR   A N    1 
ATOM   1725 C  CA   . THR   A 1 230 ? -39.500 12.495 12.658  1.00 52.75 ? 261 THR   A CA   1 
ATOM   1726 C  C    . THR   A 1 230 ? -38.219 12.063 13.353  1.00 57.73 ? 261 THR   A C    1 
ATOM   1727 O  O    . THR   A 1 230 ? -37.153 12.653 13.160  1.00 57.79 ? 261 THR   A O    1 
ATOM   1728 C  CB   . THR   A 1 230 ? -39.864 11.507 11.535  1.00 56.77 ? 261 THR   A CB   1 
ATOM   1729 O  OG1  . THR   A 1 230 ? -39.033 11.740 10.390  1.00 57.79 ? 261 THR   A OG1  1 
ATOM   1730 C  CG2  . THR   A 1 230 ? -41.322 11.674 11.129  1.00 53.28 ? 261 THR   A CG2  1 
ATOM   1731 N  N    . ALA   A 1 231 ? -38.345 11.015 14.173  1.00 55.80 ? 262 ALA   A N    1 
ATOM   1732 C  CA   . ALA   A 1 231 ? -37.274 10.628 15.088  1.00 57.62 ? 262 ALA   A CA   1 
ATOM   1733 C  C    . ALA   A 1 231 ? -35.960 10.348 14.364  1.00 56.45 ? 262 ALA   A C    1 
ATOM   1734 O  O    . ALA   A 1 231 ? -34.881 10.586 14.917  1.00 59.42 ? 262 ALA   A O    1 
ATOM   1735 C  CB   . ALA   A 1 231 ? -37.705 9.404  15.899  1.00 60.80 ? 262 ALA   A CB   1 
ATOM   1736 N  N    . ASP   A 1 232 ? -36.027 9.819  13.138  1.00 60.72 ? 263 ASP   A N    1 
ATOM   1737 C  CA   . ASP   A 1 232 ? -34.807 9.523  12.386  1.00 62.14 ? 263 ASP   A CA   1 
ATOM   1738 C  C    . ASP   A 1 232 ? -34.047 10.790 12.002  1.00 63.41 ? 263 ASP   A C    1 
ATOM   1739 O  O    . ASP   A 1 232 ? -32.833 10.736 11.765  1.00 61.10 ? 263 ASP   A O    1 
ATOM   1740 C  CB   . ASP   A 1 232 ? -35.141 8.722  11.128  1.00 56.25 ? 263 ASP   A CB   1 
ATOM   1741 C  CG   . ASP   A 1 232 ? -36.198 9.398  10.279  1.00 61.58 ? 263 ASP   A CG   1 
ATOM   1742 O  OD1  . ASP   A 1 232 ? -37.329 9.562  10.786  1.00 60.70 ? 263 ASP   A OD1  1 
ATOM   1743 O  OD2  . ASP   A 1 232 ? -35.899 9.783  9.119   1.00 63.92 ? 263 ASP   A OD2  1 
ATOM   1744 N  N    . MET   A 1 233 ? -34.744 11.929 11.917  1.00 61.15 ? 264 MET   A N    1 
ATOM   1745 C  CA   . MET   A 1 233 ? -34.145 13.211 11.556  1.00 59.96 ? 264 MET   A CA   1 
ATOM   1746 C  C    . MET   A 1 233 ? -33.476 13.912 12.731  1.00 59.78 ? 264 MET   A C    1 
ATOM   1747 O  O    . MET   A 1 233 ? -32.745 14.886 12.522  1.00 59.08 ? 264 MET   A O    1 
ATOM   1748 C  CB   . MET   A 1 233 ? -35.220 14.128 10.972  1.00 55.54 ? 264 MET   A CB   1 
ATOM   1749 C  CG   . MET   A 1 233 ? -36.064 13.471 9.905   1.00 56.34 ? 264 MET   A CG   1 
ATOM   1750 S  SD   . MET   A 1 233 ? -37.461 14.510 9.442   1.00 55.34 ? 264 MET   A SD   1 
ATOM   1751 C  CE   . MET   A 1 233 ? -36.601 16.029 9.042   1.00 50.99 ? 264 MET   A CE   1 
ATOM   1752 N  N    . ILE   A 1 234 ? -33.688 13.431 13.948  1.00 55.72 ? 265 ILE   A N    1 
ATOM   1753 C  CA   . ILE   A 1 234 ? -33.268 14.113 15.163  1.00 58.10 ? 265 ILE   A CA   1 
ATOM   1754 C  C    . ILE   A 1 234 ? -32.118 13.332 15.772  1.00 58.69 ? 265 ILE   A C    1 
ATOM   1755 O  O    . ILE   A 1 234 ? -32.110 12.097 15.737  1.00 64.94 ? 265 ILE   A O    1 
ATOM   1756 C  CB   . ILE   A 1 234 ? -34.445 14.243 16.149  1.00 55.34 ? 265 ILE   A CB   1 
ATOM   1757 C  CG1  . ILE   A 1 234 ? -35.577 15.043 15.503  1.00 57.73 ? 265 ILE   A CG1  1 
ATOM   1758 C  CG2  . ILE   A 1 234 ? -34.006 14.897 17.458  1.00 56.56 ? 265 ILE   A CG2  1 
ATOM   1759 C  CD1  . ILE   A 1 234 ? -35.163 16.445 15.093  1.00 53.55 ? 265 ILE   A CD1  1 
ATOM   1760 N  N    . LYS   A 1 235 ? -31.128 14.036 16.293  1.00 54.42 ? 266 LYS   A N    1 
ATOM   1761 C  CA   . LYS   A 1 235 ? -30.067 13.321 16.971  1.00 56.23 ? 266 LYS   A CA   1 
ATOM   1762 C  C    . LYS   A 1 235 ? -30.447 13.121 18.435  1.00 61.17 ? 266 LYS   A C    1 
ATOM   1763 O  O    . LYS   A 1 235 ? -31.251 13.869 19.000  1.00 61.16 ? 266 LYS   A O    1 
ATOM   1764 C  CB   . LYS   A 1 235 ? -28.721 14.037 16.823  1.00 53.79 ? 266 LYS   A CB   1 
ATOM   1765 C  CG   . LYS   A 1 235 ? -28.412 15.126 17.814  1.00 56.40 ? 266 LYS   A CG   1 
ATOM   1766 C  CD   . LYS   A 1 235 ? -26.939 15.528 17.689  1.00 55.35 ? 266 LYS   A CD   1 
ATOM   1767 C  CE   . LYS   A 1 235 ? -26.585 16.666 18.633  1.00 58.67 ? 266 LYS   A CE   1 
ATOM   1768 N  NZ   . LYS   A 1 235 ? -25.200 17.186 18.437  1.00 61.45 ? 266 LYS   A NZ   1 
ATOM   1769 N  N    . GLU   A 1 236 ? -29.906 12.055 19.018  1.00 61.44 ? 267 GLU   A N    1 
ATOM   1770 C  CA   . GLU   A 1 236 ? -30.193 11.666 20.393  1.00 61.61 ? 267 GLU   A CA   1 
ATOM   1771 C  C    . GLU   A 1 236 ? -29.994 12.830 21.357  1.00 58.85 ? 267 GLU   A C    1 
ATOM   1772 O  O    . GLU   A 1 236 ? -28.906 13.408 21.433  1.00 56.43 ? 267 GLU   A O    1 
ATOM   1773 C  CB   . GLU   A 1 236 ? -29.280 10.494 20.774  1.00 64.22 ? 267 GLU   A CB   1 
ATOM   1774 C  CG   . GLU   A 1 236 ? -29.624 9.795  22.073  1.00 70.98 ? 267 GLU   A CG   1 
ATOM   1775 C  CD   . GLU   A 1 236 ? -30.696 8.733  21.897  1.00 78.54 ? 267 GLU   A CD   1 
ATOM   1776 O  OE1  . GLU   A 1 236 ? -30.996 8.374  20.734  1.00 77.43 ? 267 GLU   A OE1  1 
ATOM   1777 O  OE2  . GLU   A 1 236 ? -31.238 8.262  22.922  1.00 77.86 ? 267 GLU   A OE2  1 
ATOM   1778 N  N    . GLY   A 1 237 ? -31.045 13.169 22.101  1.00 57.91 ? 268 GLY   A N    1 
ATOM   1779 C  CA   . GLY   A 1 237 ? -30.948 14.186 23.132  1.00 56.79 ? 268 GLY   A CA   1 
ATOM   1780 C  C    . GLY   A 1 237 ? -31.156 15.618 22.683  1.00 55.16 ? 268 GLY   A C    1 
ATOM   1781 O  O    . GLY   A 1 237 ? -30.968 16.534 23.494  1.00 54.87 ? 268 GLY   A O    1 
ATOM   1782 N  N    . ALA   A 1 238 ? -31.543 15.847 21.432  1.00 54.67 ? 269 ALA   A N    1 
ATOM   1783 C  CA   . ALA   A 1 238 ? -31.738 17.208 20.952  1.00 53.01 ? 269 ALA   A CA   1 
ATOM   1784 C  C    . ALA   A 1 238 ? -33.030 17.803 21.511  1.00 50.85 ? 269 ALA   A C    1 
ATOM   1785 O  O    . ALA   A 1 238 ? -33.910 17.096 22.012  1.00 49.19 ? 269 ALA   A O    1 
ATOM   1786 C  CB   . ALA   A 1 238 ? -31.765 17.247 19.421  1.00 48.35 ? 269 ALA   A CB   1 
ATOM   1787 N  N    . ALA   A 1 239 ? -33.129 19.130 21.420  1.00 44.57 ? 270 ALA   A N    1 
ATOM   1788 C  CA   . ALA   A 1 239 ? -34.319 19.869 21.816  1.00 43.58 ? 270 ALA   A CA   1 
ATOM   1789 C  C    . ALA   A 1 239 ? -35.144 20.196 20.582  1.00 44.59 ? 270 ALA   A C    1 
ATOM   1790 O  O    . ALA   A 1 239 ? -34.618 20.752 19.613  1.00 44.74 ? 270 ALA   A O    1 
ATOM   1791 C  CB   . ALA   A 1 239 ? -33.933 21.149 22.554  1.00 44.98 ? 270 ALA   A CB   1 
ATOM   1792 N  N    . VAL   A 1 240 ? -36.429 19.851 20.609  1.00 42.59 ? 271 VAL   A N    1 
ATOM   1793 C  CA   . VAL   A 1 240 ? -37.304 20.016 19.451  1.00 43.82 ? 271 VAL   A CA   1 
ATOM   1794 C  C    . VAL   A 1 240 ? -38.479 20.902 19.844  1.00 45.36 ? 271 VAL   A C    1 
ATOM   1795 O  O    . VAL   A 1 240 ? -39.281 20.532 20.711  1.00 43.16 ? 271 VAL   A O    1 
ATOM   1796 C  CB   . VAL   A 1 240 ? -37.785 18.661 18.904  1.00 41.67 ? 271 VAL   A CB   1 
ATOM   1797 C  CG1  . VAL   A 1 240 ? -38.784 18.857 17.782  1.00 43.07 ? 271 VAL   A CG1  1 
ATOM   1798 C  CG2  . VAL   A 1 240 ? -36.593 17.863 18.392  1.00 43.11 ? 271 VAL   A CG2  1 
ATOM   1799 N  N    . ILE   A 1 241 ? -38.596 22.052 19.181  1.00 39.40 ? 272 ILE   A N    1 
ATOM   1800 C  CA   . ILE   A 1 241 ? -39.591 23.068 19.500  1.00 38.48 ? 272 ILE   A CA   1 
ATOM   1801 C  C    . ILE   A 1 241 ? -40.557 23.170 18.334  1.00 42.09 ? 272 ILE   A C    1 
ATOM   1802 O  O    . ILE   A 1 241 ? -40.164 23.520 17.211  1.00 43.63 ? 272 ILE   A O    1 
ATOM   1803 C  CB   . ILE   A 1 241 ? -38.931 24.421 19.807  1.00 39.20 ? 272 ILE   A CB   1 
ATOM   1804 C  CG1  . ILE   A 1 241 ? -38.124 24.317 21.098  1.00 47.61 ? 272 ILE   A CG1  1 
ATOM   1805 C  CG2  . ILE   A 1 241 ? -39.973 25.514 19.957  1.00 39.22 ? 272 ILE   A CG2  1 
ATOM   1806 C  CD1  . ILE   A 1 241 ? -36.836 25.068 21.034  1.00 50.83 ? 272 ILE   A CD1  1 
ATOM   1807 N  N    . ASP   A 1 242 ? -41.825 22.894 18.602  1.00 39.38 ? 273 ASP   A N    1 
ATOM   1808 C  CA   . ASP   A 1 242 ? -42.824 22.710 17.557  1.00 38.36 ? 273 ASP   A CA   1 
ATOM   1809 C  C    . ASP   A 1 242 ? -43.707 23.951 17.482  1.00 40.01 ? 273 ASP   A C    1 
ATOM   1810 O  O    . ASP   A 1 242 ? -44.608 24.146 18.306  1.00 39.86 ? 273 ASP   A O    1 
ATOM   1811 C  CB   . ASP   A 1 242 ? -43.642 21.454 17.829  1.00 42.01 ? 273 ASP   A CB   1 
ATOM   1812 C  CG   . ASP   A 1 242 ? -44.366 20.952 16.597  1.00 46.71 ? 273 ASP   A CG   1 
ATOM   1813 O  OD1  . ASP   A 1 242 ? -44.540 21.746 15.641  1.00 44.08 ? 273 ASP   A OD1  1 
ATOM   1814 O  OD2  . ASP   A 1 242 ? -44.763 19.766 16.593  1.00 45.84 ? 273 ASP   A OD2  1 
ATOM   1815 N  N    . VAL   A 1 243 ? -43.458 24.784 16.468  1.00 37.59 ? 274 VAL   A N    1 
ATOM   1816 C  CA   . VAL   A 1 243 ? -44.237 26.004 16.284  1.00 37.74 ? 274 VAL   A CA   1 
ATOM   1817 C  C    . VAL   A 1 243 ? -45.490 25.775 15.441  1.00 42.71 ? 274 VAL   A C    1 
ATOM   1818 O  O    . VAL   A 1 243 ? -46.459 26.533 15.570  1.00 43.93 ? 274 VAL   A O    1 
ATOM   1819 C  CB   . VAL   A 1 243 ? -43.345 27.101 15.664  1.00 41.91 ? 274 VAL   A CB   1 
ATOM   1820 C  CG1  . VAL   A 1 243 ? -44.088 28.429 15.549  1.00 35.95 ? 274 VAL   A CG1  1 
ATOM   1821 C  CG2  . VAL   A 1 243 ? -42.036 27.255 16.482  1.00 36.39 ? 274 VAL   A CG2  1 
ATOM   1822 N  N    . GLY   A 1 244 ? -45.523 24.732 14.619  1.00 43.65 ? 275 GLY   A N    1 
ATOM   1823 C  CA   . GLY   A 1 244 ? -46.670 24.523 13.750  1.00 44.80 ? 275 GLY   A CA   1 
ATOM   1824 C  C    . GLY   A 1 244 ? -47.931 24.166 14.518  1.00 46.84 ? 275 GLY   A C    1 
ATOM   1825 O  O    . GLY   A 1 244 ? -47.891 23.528 15.573  1.00 47.27 ? 275 GLY   A O    1 
ATOM   1826 N  N    . ILE   A 1 245 ? -49.067 24.615 13.983  1.00 45.43 ? 276 ILE   A N    1 
ATOM   1827 C  CA   . ILE   A 1 245 ? -50.398 24.230 14.455  1.00 48.12 ? 276 ILE   A CA   1 
ATOM   1828 C  C    . ILE   A 1 245 ? -51.179 23.787 13.221  1.00 54.40 ? 276 ILE   A C    1 
ATOM   1829 O  O    . ILE   A 1 245 ? -51.630 24.626 12.434  1.00 56.70 ? 276 ILE   A O    1 
ATOM   1830 C  CB   . ILE   A 1 245 ? -51.120 25.368 15.183  1.00 49.65 ? 276 ILE   A CB   1 
ATOM   1831 C  CG1  . ILE   A 1 245 ? -50.286 25.854 16.367  1.00 44.17 ? 276 ILE   A CG1  1 
ATOM   1832 C  CG2  . ILE   A 1 245 ? -52.489 24.911 15.663  1.00 47.07 ? 276 ILE   A CG2  1 
ATOM   1833 C  CD1  . ILE   A 1 245 ? -50.992 26.868 17.238  1.00 45.82 ? 276 ILE   A CD1  1 
ATOM   1834 N  N    . ASN   A 1 246 ? -51.351 22.475 13.047  1.00 55.36 ? 277 ASN   A N    1 
ATOM   1835 C  CA   . ASN   A 1 246 ? -52.006 21.907 11.870  1.00 55.24 ? 277 ASN   A CA   1 
ATOM   1836 C  C    . ASN   A 1 246 ? -53.267 21.150 12.274  1.00 59.56 ? 277 ASN   A C    1 
ATOM   1837 O  O    . ASN   A 1 246 ? -53.214 20.285 13.155  1.00 57.31 ? 277 ASN   A O    1 
ATOM   1838 C  CB   . ASN   A 1 246 ? -51.060 20.962 11.130  1.00 53.74 ? 277 ASN   A CB   1 
ATOM   1839 C  CG   . ASN   A 1 246 ? -49.695 21.565 10.916  1.00 52.06 ? 277 ASN   A CG   1 
ATOM   1840 O  OD1  . ASN   A 1 246 ? -49.558 22.511 10.158  1.00 49.99 ? 277 ASN   A OD1  1 
ATOM   1841 N  ND2  . ASN   A 1 246 ? -48.677 21.027 11.595  1.00 51.23 ? 277 ASN   A ND2  1 
ATOM   1842 N  N    . ARG   A 1 247 ? -54.388 21.450 11.607  1.00 62.81 ? 278 ARG   A N    1 
ATOM   1843 C  CA   . ARG   A 1 247 ? -55.650 20.733 11.805  1.00 64.66 ? 278 ARG   A CA   1 
ATOM   1844 C  C    . ARG   A 1 247 ? -55.665 19.484 10.924  1.00 66.29 ? 278 ARG   A C    1 
ATOM   1845 O  O    . ARG   A 1 247 ? -55.702 19.584 9.693   1.00 65.15 ? 278 ARG   A O    1 
ATOM   1846 C  CB   . ARG   A 1 247 ? -56.838 21.640 11.493  1.00 63.01 ? 278 ARG   A CB   1 
ATOM   1847 N  N    . VAL   A 1 248 ? -55.647 18.308 11.551  1.00 68.61 ? 279 VAL   A N    1 
ATOM   1848 C  CA   . VAL   A 1 248 ? -55.570 17.043 10.819  1.00 68.34 ? 279 VAL   A CA   1 
ATOM   1849 C  C    . VAL   A 1 248 ? -56.726 16.105 11.180  1.00 73.81 ? 279 VAL   A C    1 
ATOM   1850 O  O    . VAL   A 1 248 ? -57.576 16.428 12.016  1.00 75.99 ? 279 VAL   A O    1 
ATOM   1851 C  CB   . VAL   A 1 248 ? -54.218 16.348 11.068  1.00 62.32 ? 279 VAL   A CB   1 
ATOM   1852 N  N    . LYS   A 1 257 ? -58.715 17.457 15.248  1.00 60.41 ? 288 LYS   A N    1 
ATOM   1853 C  CA   . LYS   A 1 257 ? -57.457 17.228 15.951  1.00 65.17 ? 288 LYS   A CA   1 
ATOM   1854 C  C    . LYS   A 1 257 ? -56.369 18.232 15.549  1.00 65.82 ? 288 LYS   A C    1 
ATOM   1855 O  O    . LYS   A 1 257 ? -56.175 18.499 14.367  1.00 64.95 ? 288 LYS   A O    1 
ATOM   1856 C  CB   . LYS   A 1 257 ? -56.956 15.807 15.691  1.00 63.32 ? 288 LYS   A CB   1 
ATOM   1857 C  CG   . LYS   A 1 257 ? -55.899 15.327 16.684  1.00 64.18 ? 288 LYS   A CG   1 
ATOM   1858 C  CD   . LYS   A 1 257 ? -55.122 14.132 16.141  1.00 64.63 ? 288 LYS   A CD   1 
ATOM   1859 C  CE   . LYS   A 1 257 ? -53.943 13.774 17.041  1.00 72.96 ? 288 LYS   A CE   1 
ATOM   1860 N  NZ   . LYS   A 1 257 ? -53.265 12.505 16.626  1.00 70.96 ? 288 LYS   A NZ   1 
ATOM   1861 N  N    . LEU   A 1 258 ? -55.656 18.774 16.536  1.00 64.83 ? 289 LEU   A N    1 
ATOM   1862 C  CA   . LEU   A 1 258 ? -54.534 19.676 16.306  1.00 56.99 ? 289 LEU   A CA   1 
ATOM   1863 C  C    . LEU   A 1 258 ? -53.223 18.957 16.580  1.00 58.50 ? 289 LEU   A C    1 
ATOM   1864 O  O    . LEU   A 1 258 ? -53.041 18.374 17.656  1.00 57.59 ? 289 LEU   A O    1 
ATOM   1865 C  CB   . LEU   A 1 258 ? -54.622 20.910 17.197  1.00 53.60 ? 289 LEU   A CB   1 
ATOM   1866 C  CG   . LEU   A 1 258 ? -55.794 21.848 16.972  1.00 55.86 ? 289 LEU   A CG   1 
ATOM   1867 C  CD1  . LEU   A 1 258 ? -55.699 23.001 17.945  1.00 54.34 ? 289 LEU   A CD1  1 
ATOM   1868 C  CD2  . LEU   A 1 258 ? -55.779 22.346 15.552  1.00 58.38 ? 289 LEU   A CD2  1 
ATOM   1869 N  N    . VAL   A 1 259 ? -52.299 19.036 15.626  1.00 51.63 ? 290 VAL   A N    1 
ATOM   1870 C  CA   . VAL   A 1 259 ? -50.950 18.516 15.786  1.00 50.00 ? 290 VAL   A CA   1 
ATOM   1871 C  C    . VAL   A 1 259 ? -49.963 19.610 15.387  1.00 48.44 ? 290 VAL   A C    1 
ATOM   1872 O  O    . VAL   A 1 259 ? -50.330 20.626 14.798  1.00 47.94 ? 290 VAL   A O    1 
ATOM   1873 C  CB   . VAL   A 1 259 ? -50.713 17.233 14.960  1.00 51.74 ? 290 VAL   A CB   1 
ATOM   1874 C  CG1  . VAL   A 1 259 ? -51.549 16.092 15.511  1.00 54.40 ? 290 VAL   A CG1  1 
ATOM   1875 C  CG2  . VAL   A 1 259 ? -51.044 17.475 13.489  1.00 52.54 ? 290 VAL   A CG2  1 
ATOM   1876 N  N    . GLY   A 1 260 ? -48.699 19.406 15.755  1.00 46.84 ? 291 GLY   A N    1 
ATOM   1877 C  CA   . GLY   A 1 260 ? -47.620 20.266 15.321  1.00 48.23 ? 291 GLY   A CA   1 
ATOM   1878 C  C    . GLY   A 1 260 ? -46.974 19.743 14.047  1.00 51.13 ? 291 GLY   A C    1 
ATOM   1879 O  O    . GLY   A 1 260 ? -47.480 18.837 13.381  1.00 51.39 ? 291 GLY   A O    1 
ATOM   1880 N  N    . ASP   A 1 261 ? -45.824 20.334 13.708  1.00 46.95 ? 292 ASP   A N    1 
ATOM   1881 C  CA   . ASP   A 1 261 ? -45.031 19.824 12.593  1.00 50.81 ? 292 ASP   A CA   1 
ATOM   1882 C  C    . ASP   A 1 261 ? -44.297 18.545 12.945  1.00 49.55 ? 292 ASP   A C    1 
ATOM   1883 O  O    . ASP   A 1 261 ? -43.784 17.875 12.046  1.00 48.28 ? 292 ASP   A O    1 
ATOM   1884 C  CB   . ASP   A 1 261 ? -43.974 20.828 12.147  1.00 43.48 ? 292 ASP   A CB   1 
ATOM   1885 C  CG   . ASP   A 1 261 ? -44.550 22.108 11.647  1.00 43.99 ? 292 ASP   A CG   1 
ATOM   1886 O  OD1  . ASP   A 1 261 ? -43.755 23.066 11.523  1.00 44.94 ? 292 ASP   A OD1  1 
ATOM   1887 O  OD2  . ASP   A 1 261 ? -45.776 22.167 11.380  1.00 44.26 ? 292 ASP   A OD2  1 
ATOM   1888 N  N    . VAL   A 1 262 ? -44.186 18.233 14.226  1.00 45.95 ? 293 VAL   A N    1 
ATOM   1889 C  CA   . VAL   A 1 262 ? -43.350 17.146 14.709  1.00 48.67 ? 293 VAL   A CA   1 
ATOM   1890 C  C    . VAL   A 1 262 ? -44.214 15.918 14.953  1.00 51.61 ? 293 VAL   A C    1 
ATOM   1891 O  O    . VAL   A 1 262 ? -45.347 16.022 15.439  1.00 52.23 ? 293 VAL   A O    1 
ATOM   1892 C  CB   . VAL   A 1 262 ? -42.609 17.571 15.993  1.00 47.90 ? 293 VAL   A CB   1 
ATOM   1893 C  CG1  . VAL   A 1 262 ? -41.785 16.426 16.567  1.00 49.88 ? 293 VAL   A CG1  1 
ATOM   1894 C  CG2  . VAL   A 1 262 ? -41.740 18.780 15.707  1.00 47.77 ? 293 VAL   A CG2  1 
ATOM   1895 N  N    . ASP   A 1 263 ? -43.676 14.751 14.613  1.00 54.33 ? 294 ASP   A N    1 
ATOM   1896 C  CA   . ASP   A 1 263 ? -44.264 13.493 15.052  1.00 57.11 ? 294 ASP   A CA   1 
ATOM   1897 C  C    . ASP   A 1 263 ? -44.051 13.404 16.556  1.00 53.80 ? 294 ASP   A C    1 
ATOM   1898 O  O    . ASP   A 1 263 ? -42.997 12.943 17.009  1.00 53.44 ? 294 ASP   A O    1 
ATOM   1899 C  CB   . ASP   A 1 263 ? -43.609 12.311 14.325  1.00 57.20 ? 294 ASP   A CB   1 
ATOM   1900 C  CG   . ASP   A 1 263 ? -44.127 10.952 14.799  1.00 61.17 ? 294 ASP   A CG   1 
ATOM   1901 O  OD1  . ASP   A 1 263 ? -43.727 9.939  14.186  1.00 58.99 ? 294 ASP   A OD1  1 
ATOM   1902 O  OD2  . ASP   A 1 263 ? -44.937 10.889 15.756  1.00 59.23 ? 294 ASP   A OD2  1 
ATOM   1903 N  N    . PHE   A 1 264 ? -45.035 13.857 17.337  1.00 52.08 ? 295 PHE   A N    1 
ATOM   1904 C  CA   . PHE   A 1 264 ? -44.793 14.034 18.766  1.00 54.62 ? 295 PHE   A CA   1 
ATOM   1905 C  C    . PHE   A 1 264 ? -44.361 12.726 19.416  1.00 60.71 ? 295 PHE   A C    1 
ATOM   1906 O  O    . PHE   A 1 264 ? -43.327 12.674 20.092  1.00 59.38 ? 295 PHE   A O    1 
ATOM   1907 C  CB   . PHE   A 1 264 ? -46.028 14.599 19.465  1.00 53.72 ? 295 PHE   A CB   1 
ATOM   1908 C  CG   . PHE   A 1 264 ? -45.802 14.896 20.932  1.00 59.99 ? 295 PHE   A CG   1 
ATOM   1909 C  CD1  . PHE   A 1 264 ? -46.348 14.085 21.915  1.00 59.23 ? 295 PHE   A CD1  1 
ATOM   1910 C  CD2  . PHE   A 1 264 ? -45.017 15.970 21.324  1.00 53.63 ? 295 PHE   A CD2  1 
ATOM   1911 C  CE1  . PHE   A 1 264 ? -46.130 14.351 23.256  1.00 60.58 ? 295 PHE   A CE1  1 
ATOM   1912 C  CE2  . PHE   A 1 264 ? -44.797 16.242 22.664  1.00 55.74 ? 295 PHE   A CE2  1 
ATOM   1913 C  CZ   . PHE   A 1 264 ? -45.351 15.431 23.631  1.00 56.93 ? 295 PHE   A CZ   1 
ATOM   1914 N  N    . GLU   A 1 265 ? -45.112 11.644 19.176  1.00 62.10 ? 296 GLU   A N    1 
ATOM   1915 C  CA   . GLU   A 1 265 ? -44.848 10.388 19.876  1.00 63.72 ? 296 GLU   A CA   1 
ATOM   1916 C  C    . GLU   A 1 265 ? -43.505 9.779  19.477  1.00 61.87 ? 296 GLU   A C    1 
ATOM   1917 O  O    . GLU   A 1 265 ? -42.785 9.249  20.331  1.00 60.92 ? 296 GLU   A O    1 
ATOM   1918 C  CB   . GLU   A 1 265 ? -45.992 9.404  19.632  1.00 62.58 ? 296 GLU   A CB   1 
ATOM   1919 C  CG   . GLU   A 1 265 ? -47.350 9.889  20.161  1.00 62.63 ? 296 GLU   A CG   1 
ATOM   1920 C  CD   . GLU   A 1 265 ? -47.346 10.208 21.662  1.00 69.29 ? 296 GLU   A CD   1 
ATOM   1921 O  OE1  . GLU   A 1 265 ? -48.225 10.981 22.105  1.00 70.35 ? 296 GLU   A OE1  1 
ATOM   1922 O  OE2  . GLU   A 1 265 ? -46.474 9.696  22.401  1.00 67.26 ? 296 GLU   A OE2  1 
ATOM   1923 N  N    . GLY   A 1 266 ? -43.150 9.838  18.191  1.00 60.87 ? 297 GLY   A N    1 
ATOM   1924 C  CA   . GLY   A 1 266 ? -41.893 9.241  17.760  1.00 57.52 ? 297 GLY   A CA   1 
ATOM   1925 C  C    . GLY   A 1 266 ? -40.672 9.999  18.255  1.00 59.31 ? 297 GLY   A C    1 
ATOM   1926 O  O    . GLY   A 1 266 ? -39.732 9.405  18.792  1.00 59.86 ? 297 GLY   A O    1 
ATOM   1927 N  N    . VAL   A 1 267 ? -40.669 11.324 18.074  1.00 60.79 ? 298 VAL   A N    1 
ATOM   1928 C  CA   . VAL   A 1 267 ? -39.513 12.148 18.433  1.00 59.64 ? 298 VAL   A CA   1 
ATOM   1929 C  C    . VAL   A 1 267 ? -39.318 12.176 19.945  1.00 58.06 ? 298 VAL   A C    1 
ATOM   1930 O  O    . VAL   A 1 267 ? -38.185 12.274 20.441  1.00 57.57 ? 298 VAL   A O    1 
ATOM   1931 C  CB   . VAL   A 1 267 ? -39.696 13.561 17.842  1.00 57.88 ? 298 VAL   A CB   1 
ATOM   1932 C  CG1  . VAL   A 1 267 ? -38.645 14.529 18.390  1.00 51.73 ? 298 VAL   A CG1  1 
ATOM   1933 C  CG2  . VAL   A 1 267 ? -39.667 13.499 16.305  1.00 55.39 ? 298 VAL   A CG2  1 
ATOM   1934 N  N    . ARG   A 1 268 ? -40.419 12.092 20.691  1.00 60.57 ? 299 ARG   A N    1 
ATOM   1935 C  CA   . ARG   A 1 268 ? -40.501 11.917 22.139  1.00 57.23 ? 299 ARG   A CA   1 
ATOM   1936 C  C    . ARG   A 1 268 ? -39.547 10.857 22.675  1.00 61.91 ? 299 ARG   A C    1 
ATOM   1937 O  O    . ARG   A 1 268 ? -39.093 10.933 23.825  1.00 65.56 ? 299 ARG   A O    1 
ATOM   1938 C  CB   . ARG   A 1 268 ? -41.944 11.539 22.446  1.00 62.65 ? 299 ARG   A CB   1 
ATOM   1939 C  CG   . ARG   A 1 268 ? -42.450 11.565 23.839  1.00 66.52 ? 299 ARG   A CG   1 
ATOM   1940 C  CD   . ARG   A 1 268 ? -43.674 10.648 23.792  1.00 68.20 ? 299 ARG   A CD   1 
ATOM   1941 N  NE   . ARG   A 1 268 ? -44.802 11.073 24.608  1.00 69.90 ? 299 ARG   A NE   1 
ATOM   1942 C  CZ   . ARG   A 1 268 ? -44.722 11.430 25.880  1.00 71.76 ? 299 ARG   A CZ   1 
ATOM   1943 N  NH1  . ARG   A 1 268 ? -43.595 11.310 26.561  1.00 74.52 ? 299 ARG   A NH1  1 
ATOM   1944 N  NH2  . ARG   A 1 268 ? -45.801 11.906 26.487  1.00 71.64 ? 299 ARG   A NH2  1 
ATOM   1945 N  N    . GLN   A 1 269 ? -39.257 9.849  21.847  1.00 63.27 ? 300 GLN   A N    1 
ATOM   1946 C  CA   . GLN   A 1 269 ? -38.390 8.746  22.231  1.00 63.92 ? 300 GLN   A CA   1 
ATOM   1947 C  C    . GLN   A 1 269 ? -36.915 9.034  22.001  1.00 64.66 ? 300 GLN   A C    1 
ATOM   1948 O  O    . GLN   A 1 269 ? -36.068 8.368  22.606  1.00 65.01 ? 300 GLN   A O    1 
ATOM   1949 C  CB   . GLN   A 1 269 ? -38.791 7.480  21.465  1.00 65.37 ? 300 GLN   A CB   1 
ATOM   1950 C  CG   . GLN   A 1 269 ? -40.146 6.910  21.887  1.00 67.87 ? 300 GLN   A CG   1 
ATOM   1951 C  CD   . GLN   A 1 269 ? -40.262 6.725  23.404  1.00 73.23 ? 300 GLN   A CD   1 
ATOM   1952 O  OE1  . GLN   A 1 269 ? -41.276 7.081  24.015  1.00 72.57 ? 300 GLN   A OE1  1 
ATOM   1953 N  NE2  . GLN   A 1 269 ? -39.222 6.160  24.013  1.00 71.49 ? 300 GLN   A NE2  1 
ATOM   1954 N  N    . LYS   A 1 270 ? -36.579 10.007 21.170  1.00 62.16 ? 301 LYS   A N    1 
ATOM   1955 C  CA   . LYS   A 1 270 ? -35.172 10.276 20.917  1.00 62.55 ? 301 LYS   A CA   1 
ATOM   1956 C  C    . LYS   A 1 270 ? -34.730 11.656 21.377  1.00 62.26 ? 301 LYS   A C    1 
ATOM   1957 O  O    . LYS   A 1 270 ? -33.587 11.819 21.813  1.00 60.12 ? 301 LYS   A O    1 
ATOM   1958 C  CB   . LYS   A 1 270 ? -34.871 10.092 19.428  1.00 63.66 ? 301 LYS   A CB   1 
ATOM   1959 C  CG   . LYS   A 1 270 ? -33.411 10.104 19.085  1.00 66.87 ? 301 LYS   A CG   1 
ATOM   1960 C  CD   . LYS   A 1 270 ? -33.179 9.100  18.009  1.00 63.56 ? 301 LYS   A CD   1 
ATOM   1961 C  CE   . LYS   A 1 270 ? -32.659 9.739  16.752  1.00 66.03 ? 301 LYS   A CE   1 
ATOM   1962 N  NZ   . LYS   A 1 270 ? -32.957 8.868  15.575  1.00 65.99 ? 301 LYS   A NZ   1 
ATOM   1963 N  N    . ALA   A 1 271 ? -35.610 12.651 21.325  1.00 61.79 ? 302 ALA   A N    1 
ATOM   1964 C  CA   . ALA   A 1 271 ? -35.256 13.992 21.773  1.00 57.47 ? 302 ALA   A CA   1 
ATOM   1965 C  C    . ALA   A 1 271 ? -34.993 14.029 23.278  1.00 56.24 ? 302 ALA   A C    1 
ATOM   1966 O  O    . ALA   A 1 271 ? -35.515 13.215 24.044  1.00 57.27 ? 302 ALA   A O    1 
ATOM   1967 C  CB   . ALA   A 1 271 ? -36.370 14.978 21.426  1.00 53.12 ? 302 ALA   A CB   1 
ATOM   1968 N  N    . GLY   A 1 272 ? -34.157 14.983 23.696  1.00 49.69 ? 303 GLY   A N    1 
ATOM   1969 C  CA   . GLY   A 1 272 ? -34.036 15.287 25.111  1.00 51.07 ? 303 GLY   A CA   1 
ATOM   1970 C  C    . GLY   A 1 272 ? -35.118 16.215 25.629  1.00 52.78 ? 303 GLY   A C    1 
ATOM   1971 O  O    . GLY   A 1 272 ? -35.520 16.116 26.795  1.00 52.08 ? 303 GLY   A O    1 
ATOM   1972 N  N    . TYR   A 1 273 ? -35.601 17.124 24.780  1.00 53.44 ? 304 TYR   A N    1 
ATOM   1973 C  CA   . TYR   A 1 273 ? -36.666 18.062 25.108  1.00 47.22 ? 304 TYR   A CA   1 
ATOM   1974 C  C    . TYR   A 1 273 ? -37.615 18.156 23.931  1.00 47.74 ? 304 TYR   A C    1 
ATOM   1975 O  O    . TYR   A 1 273 ? -37.213 17.981 22.777  1.00 48.34 ? 304 TYR   A O    1 
ATOM   1976 C  CB   . TYR   A 1 273 ? -36.149 19.461 25.401  1.00 45.19 ? 304 TYR   A CB   1 
ATOM   1977 C  CG   . TYR   A 1 273 ? -35.398 19.580 26.670  1.00 47.17 ? 304 TYR   A CG   1 
ATOM   1978 C  CD1  . TYR   A 1 273 ? -36.069 19.777 27.870  1.00 51.48 ? 304 TYR   A CD1  1 
ATOM   1979 C  CD2  . TYR   A 1 273 ? -34.014 19.515 26.686  1.00 50.61 ? 304 TYR   A CD2  1 
ATOM   1980 C  CE1  . TYR   A 1 273 ? -35.382 19.897 29.064  1.00 51.16 ? 304 TYR   A CE1  1 
ATOM   1981 C  CE2  . TYR   A 1 273 ? -33.313 19.640 27.876  1.00 52.65 ? 304 TYR   A CE2  1 
ATOM   1982 C  CZ   . TYR   A 1 273 ? -34.005 19.827 29.060  1.00 51.48 ? 304 TYR   A CZ   1 
ATOM   1983 O  OH   . TYR   A 1 273 ? -33.320 19.955 30.242  1.00 57.48 ? 304 TYR   A OH   1 
ATOM   1984 N  N    . ILE   A 1 274 ? -38.875 18.468 24.223  1.00 43.49 ? 305 ILE   A N    1 
ATOM   1985 C  CA   . ILE   A 1 274 ? -39.874 18.556 23.171  1.00 44.86 ? 305 ILE   A CA   1 
ATOM   1986 C  C    . ILE   A 1 274 ? -41.005 19.434 23.670  1.00 42.91 ? 305 ILE   A C    1 
ATOM   1987 O  O    . ILE   A 1 274 ? -41.316 19.450 24.866  1.00 46.27 ? 305 ILE   A O    1 
ATOM   1988 C  CB   . ILE   A 1 274 ? -40.355 17.143 22.750  1.00 49.22 ? 305 ILE   A CB   1 
ATOM   1989 C  CG1  . ILE   A 1 274 ? -41.135 17.201 21.440  1.00 40.91 ? 305 ILE   A CG1  1 
ATOM   1990 C  CG2  . ILE   A 1 274 ? -41.179 16.470 23.872  1.00 43.54 ? 305 ILE   A CG2  1 
ATOM   1991 C  CD1  . ILE   A 1 274 ? -41.394 15.835 20.844  1.00 49.31 ? 305 ILE   A CD1  1 
ATOM   1992 N  N    . THR   A 1 275 ? -41.593 20.203 22.758  1.00 40.45 ? 306 THR   A N    1 
ATOM   1993 C  CA   . THR   A 1 275 ? -42.783 20.940 23.131  1.00 41.50 ? 306 THR   A CA   1 
ATOM   1994 C  C    . THR   A 1 275 ? -44.000 20.295 22.485  1.00 44.11 ? 306 THR   A C    1 
ATOM   1995 O  O    . THR   A 1 275 ? -43.915 19.796 21.356  1.00 45.38 ? 306 THR   A O    1 
ATOM   1996 C  CB   . THR   A 1 275 ? -42.718 22.425 22.727  1.00 41.47 ? 306 THR   A CB   1 
ATOM   1997 O  OG1  . THR   A 1 275 ? -42.542 22.548 21.304  1.00 41.60 ? 306 THR   A OG1  1 
ATOM   1998 C  CG2  . THR   A 1 275 ? -41.580 23.122 23.440  1.00 38.09 ? 306 THR   A CG2  1 
ATOM   1999 N  N    . PRO   A 1 276 ? -45.129 20.256 23.186  1.00 47.92 ? 307 PRO   A N    1 
ATOM   2000 C  CA   . PRO   A 1 276 ? -46.343 19.667 22.622  1.00 47.58 ? 307 PRO   A CA   1 
ATOM   2001 C  C    . PRO   A 1 276 ? -47.149 20.685 21.827  1.00 44.32 ? 307 PRO   A C    1 
ATOM   2002 O  O    . PRO   A 1 276 ? -46.992 21.898 21.969  1.00 41.02 ? 307 PRO   A O    1 
ATOM   2003 C  CB   . PRO   A 1 276 ? -47.114 19.228 23.874  1.00 47.94 ? 307 PRO   A CB   1 
ATOM   2004 C  CG   . PRO   A 1 276 ? -46.771 20.296 24.872  1.00 46.71 ? 307 PRO   A CG   1 
ATOM   2005 C  CD   . PRO   A 1 276 ? -45.328 20.684 24.585  1.00 43.03 ? 307 PRO   A CD   1 
ATOM   2006 N  N    . VAL   A 1 277 ? -48.033 20.160 20.984  1.00 43.52 ? 308 VAL   A N    1 
ATOM   2007 C  CA   . VAL   A 1 277 ? -49.051 20.973 20.326  1.00 44.51 ? 308 VAL   A CA   1 
ATOM   2008 C  C    . VAL   A 1 277 ? -50.402 20.289 20.499  1.00 43.34 ? 308 VAL   A C    1 
ATOM   2009 O  O    . VAL   A 1 277 ? -50.537 19.106 20.166  1.00 44.19 ? 308 VAL   A O    1 
ATOM   2010 C  CB   . VAL   A 1 277 ? -48.727 21.188 18.839  1.00 42.70 ? 308 VAL   A CB   1 
ATOM   2011 C  CG1  . VAL   A 1 277 ? -49.807 22.015 18.189  1.00 39.85 ? 308 VAL   A CG1  1 
ATOM   2012 C  CG2  . VAL   A 1 277 ? -47.378 21.865 18.692  1.00 40.77 ? 308 VAL   A CG2  1 
ATOM   2013 N  N    . PRO   A 1 278 ? -51.430 20.983 21.002  1.00 42.06 ? 309 PRO   A N    1 
ATOM   2014 C  CA   . PRO   A 1 278 ? -51.351 22.357 21.502  1.00 41.27 ? 309 PRO   A CA   1 
ATOM   2015 C  C    . PRO   A 1 278 ? -50.658 22.458 22.863  1.00 43.74 ? 309 PRO   A C    1 
ATOM   2016 O  O    . PRO   A 1 278 ? -50.083 21.472 23.331  1.00 42.74 ? 309 PRO   A O    1 
ATOM   2017 C  CB   . PRO   A 1 278 ? -52.822 22.773 21.607  1.00 45.14 ? 309 PRO   A CB   1 
ATOM   2018 C  CG   . PRO   A 1 278 ? -53.576 21.503 21.704  1.00 49.00 ? 309 PRO   A CG   1 
ATOM   2019 C  CD   . PRO   A 1 278 ? -52.824 20.538 20.850  1.00 44.76 ? 309 PRO   A CD   1 
ATOM   2020 N  N    . GLY   A 1 279 ? -50.692 23.646 23.468  1.00 43.78 ? 310 GLY   A N    1 
ATOM   2021 C  CA   . GLY   A 1 279 ? -50.098 23.848 24.779  1.00 38.39 ? 310 GLY   A CA   1 
ATOM   2022 C  C    . GLY   A 1 279 ? -48.597 24.029 24.790  1.00 40.33 ? 310 GLY   A C    1 
ATOM   2023 O  O    . GLY   A 1 279 ? -47.974 23.884 25.845  1.00 36.15 ? 310 GLY   A O    1 
ATOM   2024 N  N    . GLY   A 1 280 ? -47.985 24.345 23.647  1.00 39.77 ? 311 GLY   A N    1 
ATOM   2025 C  CA   . GLY   A 1 280 ? -46.548 24.528 23.633  1.00 34.02 ? 311 GLY   A CA   1 
ATOM   2026 C  C    . GLY   A 1 280 ? -46.142 25.957 23.339  1.00 39.64 ? 311 GLY   A C    1 
ATOM   2027 O  O    . GLY   A 1 280 ? -46.238 26.832 24.207  1.00 34.10 ? 311 GLY   A O    1 
ATOM   2028 N  N    . VAL   A 1 281 ? -45.702 26.210 22.101  1.00 32.45 ? 312 VAL   A N    1 
ATOM   2029 C  CA   . VAL   A 1 281 ? -45.307 27.564 21.719  1.00 32.31 ? 312 VAL   A CA   1 
ATOM   2030 C  C    . VAL   A 1 281 ? -46.505 28.514 21.749  1.00 30.00 ? 312 VAL   A C    1 
ATOM   2031 O  O    . VAL   A 1 281 ? -46.366 29.700 22.076  1.00 34.15 ? 312 VAL   A O    1 
ATOM   2032 C  CB   . VAL   A 1 281 ? -44.632 27.528 20.328  1.00 35.51 ? 312 VAL   A CB   1 
ATOM   2033 C  CG1  . VAL   A 1 281 ? -44.459 28.930 19.775  1.00 32.71 ? 312 VAL   A CG1  1 
ATOM   2034 C  CG2  . VAL   A 1 281 ? -43.284 26.796 20.415  1.00 32.77 ? 312 VAL   A CG2  1 
ATOM   2035 N  N    . GLY   A 1 282 ? -47.690 28.027 21.385  1.00 33.22 ? 313 GLY   A N    1 
ATOM   2036 C  CA   . GLY   A 1 282 ? -48.876 28.861 21.311  1.00 32.40 ? 313 GLY   A CA   1 
ATOM   2037 C  C    . GLY   A 1 282 ? -49.110 29.718 22.547  1.00 36.38 ? 313 GLY   A C    1 
ATOM   2038 O  O    . GLY   A 1 282 ? -49.197 30.952 22.467  1.00 33.50 ? 313 GLY   A O    1 
ATOM   2039 N  N    . PRO   A 1 283 ? -49.235 29.083 23.723  1.00 34.25 ? 314 PRO   A N    1 
ATOM   2040 C  CA   . PRO   A 1 283 ? -49.414 29.879 24.947  1.00 31.70 ? 314 PRO   A CA   1 
ATOM   2041 C  C    . PRO   A 1 283 ? -48.271 30.850 25.184  1.00 30.57 ? 314 PRO   A C    1 
ATOM   2042 O  O    . PRO   A 1 283 ? -48.490 31.957 25.695  1.00 31.16 ? 314 PRO   A O    1 
ATOM   2043 C  CB   . PRO   A 1 283 ? -49.496 28.812 26.054  1.00 34.93 ? 314 PRO   A CB   1 
ATOM   2044 C  CG   . PRO   A 1 283 ? -50.003 27.604 25.373  1.00 38.16 ? 314 PRO   A CG   1 
ATOM   2045 C  CD   . PRO   A 1 283 ? -49.363 27.641 23.983  1.00 32.89 ? 314 PRO   A CD   1 
ATOM   2046 N  N    . MET   A 1 284 ? -47.054 30.477 24.795  1.00 32.01 ? 315 MET   A N    1 
ATOM   2047 C  CA   . MET   A 1 284 ? -45.921 31.380 24.967  1.00 29.22 ? 315 MET   A CA   1 
ATOM   2048 C  C    . MET   A 1 284 ? -46.052 32.615 24.091  1.00 30.59 ? 315 MET   A C    1 
ATOM   2049 O  O    . MET   A 1 284 ? -45.650 33.700 24.515  1.00 29.99 ? 315 MET   A O    1 
ATOM   2050 C  CB   . MET   A 1 284 ? -44.626 30.641 24.666  1.00 30.22 ? 315 MET   A CB   1 
ATOM   2051 C  CG   . MET   A 1 284 ? -44.273 29.607 25.712  1.00 30.54 ? 315 MET   A CG   1 
ATOM   2052 S  SD   . MET   A 1 284 ? -43.970 30.456 27.277  1.00 36.47 ? 315 MET   A SD   1 
ATOM   2053 C  CE   . MET   A 1 284 ? -42.453 31.321 26.896  1.00 33.06 ? 315 MET   A CE   1 
ATOM   2054 N  N    . THR   A 1 285 ? -46.621 32.477 22.876  1.00 29.88 ? 316 THR   A N    1 
ATOM   2055 C  CA   . THR   A 1 285 ? -46.891 33.658 22.054  1.00 28.02 ? 316 THR   A CA   1 
ATOM   2056 C  C    . THR   A 1 285 ? -47.764 34.648 22.794  1.00 30.88 ? 316 THR   A C    1 
ATOM   2057 O  O    . THR   A 1 285 ? -47.511 35.860 22.784  1.00 30.26 ? 316 THR   A O    1 
ATOM   2058 C  CB   . THR   A 1 285 ? -47.595 33.269 20.756  1.00 28.81 ? 316 THR   A CB   1 
ATOM   2059 O  OG1  . THR   A 1 285 ? -46.756 32.388 20.018  1.00 31.36 ? 316 THR   A OG1  1 
ATOM   2060 C  CG2  . THR   A 1 285 ? -47.917 34.530 19.950  1.00 30.28 ? 316 THR   A CG2  1 
ATOM   2061 N  N    . VAL   A 1 286 ? -48.827 34.151 23.411  1.00 29.53 ? 317 VAL   A N    1 
ATOM   2062 C  CA   . VAL   A 1 286 ? -49.739 35.044 24.105  1.00 27.24 ? 317 VAL   A CA   1 
ATOM   2063 C  C    . VAL   A 1 286 ? -49.046 35.701 25.296  1.00 27.64 ? 317 VAL   A C    1 
ATOM   2064 O  O    . VAL   A 1 286 ? -49.227 36.898 25.546  1.00 29.01 ? 317 VAL   A O    1 
ATOM   2065 C  CB   . VAL   A 1 286 ? -51.001 34.270 24.516  1.00 30.33 ? 317 VAL   A CB   1 
ATOM   2066 C  CG1  . VAL   A 1 286 ? -51.891 35.140 25.340  1.00 29.64 ? 317 VAL   A CG1  1 
ATOM   2067 C  CG2  . VAL   A 1 286 ? -51.750 33.781 23.256  1.00 31.43 ? 317 VAL   A CG2  1 
ATOM   2068 N  N    . ALA   A 1 287 ? -48.240 34.942 26.049  1.00 28.60 ? 318 ALA   A N    1 
ATOM   2069 C  CA   . ALA   A 1 287 ? -47.575 35.548 27.211  1.00 31.63 ? 318 ALA   A CA   1 
ATOM   2070 C  C    . ALA   A 1 287 ? -46.569 36.615 26.782  1.00 31.23 ? 318 ALA   A C    1 
ATOM   2071 O  O    . ALA   A 1 287 ? -46.480 37.670 27.417  1.00 32.39 ? 318 ALA   A O    1 
ATOM   2072 C  CB   . ALA   A 1 287 ? -46.897 34.478 28.070  1.00 30.19 ? 318 ALA   A CB   1 
ATOM   2073 N  N    . MET   A 1 288 ? -45.824 36.390 25.686  1.00 29.86 ? 319 MET   A N    1 
ATOM   2074 C  CA   . MET   A 1 288 ? -44.851 37.416 25.307  1.00 31.61 ? 319 MET   A CA   1 
ATOM   2075 C  C    . MET   A 1 288 ? -45.533 38.679 24.773  1.00 31.90 ? 319 MET   A C    1 
ATOM   2076 O  O    . MET   A 1 288 ? -44.982 39.778 24.913  1.00 29.63 ? 319 MET   A O    1 
ATOM   2077 C  CB   . MET   A 1 288 ? -43.837 36.863 24.300  1.00 29.94 ? 319 MET   A CB   1 
ATOM   2078 C  CG   . MET   A 1 288 ? -43.026 35.688 24.842  1.00 30.34 ? 319 MET   A CG   1 
ATOM   2079 S  SD   . MET   A 1 288 ? -42.607 35.784 26.618  1.00 36.04 ? 319 MET   A SD   1 
ATOM   2080 C  CE   . MET   A 1 288 ? -41.076 36.716 26.613  1.00 30.61 ? 319 MET   A CE   1 
ATOM   2081 N  N    . LEU   A 1 289 ? -46.742 38.562 24.206  1.00 29.28 ? 320 LEU   A N    1 
ATOM   2082 C  CA   . LEU   A 1 289 ? -47.492 39.763 23.831  1.00 27.62 ? 320 LEU   A CA   1 
ATOM   2083 C  C    . LEU   A 1 289 ? -47.826 40.618 25.054  1.00 28.19 ? 320 LEU   A C    1 
ATOM   2084 O  O    . LEU   A 1 289 ? -47.738 41.857 25.009  1.00 29.18 ? 320 LEU   A O    1 
ATOM   2085 C  CB   . LEU   A 1 289 ? -48.776 39.377 23.105  1.00 30.24 ? 320 LEU   A CB   1 
ATOM   2086 C  CG   . LEU   A 1 289 ? -49.738 40.542 22.855  1.00 34.37 ? 320 LEU   A CG   1 
ATOM   2087 C  CD1  . LEU   A 1 289 ? -49.151 41.505 21.834  1.00 37.82 ? 320 LEU   A CD1  1 
ATOM   2088 C  CD2  . LEU   A 1 289 ? -51.059 40.020 22.349  1.00 34.17 ? 320 LEU   A CD2  1 
ATOM   2089 N  N    . MET   A 1 290 ? -48.255 39.977 26.145  1.00 31.04 ? 321 MET   A N    1 
ATOM   2090 C  CA   . MET   A 1 290 ? -48.507 40.704 27.392  1.00 30.56 ? 321 MET   A CA   1 
ATOM   2091 C  C    . MET   A 1 290 ? -47.252 41.435 27.870  1.00 28.80 ? 321 MET   A C    1 
ATOM   2092 O  O    . MET   A 1 290 ? -47.321 42.604 28.272  1.00 31.52 ? 321 MET   A O    1 
ATOM   2093 C  CB   . MET   A 1 290 ? -49.004 39.734 28.470  1.00 29.14 ? 321 MET   A CB   1 
ATOM   2094 C  CG   . MET   A 1 290 ? -50.228 38.907 28.077  1.00 29.43 ? 321 MET   A CG   1 
ATOM   2095 S  SD   . MET   A 1 290 ? -51.653 39.942 27.674  1.00 36.02 ? 321 MET   A SD   1 
ATOM   2096 C  CE   . MET   A 1 290 ? -51.605 39.880 25.855  1.00 31.67 ? 321 MET   A CE   1 
ATOM   2097 N  N    . LYS   A 1 291 ? -46.093 40.772 27.804  1.00 29.17 ? 322 LYS   A N    1 
ATOM   2098 C  CA   . LYS   A 1 291 ? -44.824 41.441 28.107  1.00 30.97 ? 322 LYS   A CA   1 
ATOM   2099 C  C    . LYS   A 1 291 ? -44.624 42.673 27.235  1.00 35.67 ? 322 LYS   A C    1 
ATOM   2100 O  O    . LYS   A 1 291 ? -44.231 43.732 27.737  1.00 30.57 ? 322 LYS   A O    1 
ATOM   2101 C  CB   . LYS   A 1 291 ? -43.641 40.478 27.920  1.00 35.89 ? 322 LYS   A CB   1 
ATOM   2102 C  CG   . LYS   A 1 291 ? -43.412 39.475 29.053  1.00 40.54 ? 322 LYS   A CG   1 
ATOM   2103 C  CD   . LYS   A 1 291 ? -42.855 40.140 30.307  1.00 49.68 ? 322 LYS   A CD   1 
ATOM   2104 C  CE   . LYS   A 1 291 ? -41.334 40.304 30.285  1.00 60.11 ? 322 LYS   A CE   1 
ATOM   2105 N  NZ   . LYS   A 1 291 ? -40.582 39.012 30.460  1.00 59.96 ? 322 LYS   A NZ   1 
ATOM   2106 N  N    . ASN   A 1 292 ? -44.881 42.548 25.910  1.00 30.23 ? 323 ASN   A N    1 
ATOM   2107 C  CA   . ASN   A 1 292 ? -44.703 43.682 25.003  1.00 31.33 ? 323 ASN   A CA   1 
ATOM   2108 C  C    . ASN   A 1 292 ? -45.664 44.814 25.328  1.00 29.81 ? 323 ASN   A C    1 
ATOM   2109 O  O    . ASN   A 1 292 ? -45.337 45.993 25.141  1.00 34.30 ? 323 ASN   A O    1 
ATOM   2110 C  CB   . ASN   A 1 292 ? -44.914 43.258 23.536  1.00 30.56 ? 323 ASN   A CB   1 
ATOM   2111 C  CG   . ASN   A 1 292 ? -43.718 42.546 22.957  1.00 34.43 ? 323 ASN   A CG   1 
ATOM   2112 O  OD1  . ASN   A 1 292 ? -42.664 42.474 23.592  1.00 34.92 ? 323 ASN   A OD1  1 
ATOM   2113 N  ND2  . ASN   A 1 292 ? -43.854 42.050 21.717  1.00 34.22 ? 323 ASN   A ND2  1 
ATOM   2114 N  N    . THR   A 1 293 ? -46.880 44.479 25.735  1.00 27.52 ? 324 THR   A N    1 
ATOM   2115 C  CA   . THR   A 1 293 ? -47.874 45.523 25.981  1.00 29.77 ? 324 THR   A CA   1 
ATOM   2116 C  C    . THR   A 1 293 ? -47.484 46.408 27.177  1.00 35.73 ? 324 THR   A C    1 
ATOM   2117 O  O    . THR   A 1 293 ? -47.624 47.640 27.123  1.00 33.47 ? 324 THR   A O    1 
ATOM   2118 C  CB   . THR   A 1 293 ? -49.253 44.881 26.193  1.00 31.02 ? 324 THR   A CB   1 
ATOM   2119 O  OG1  . THR   A 1 293 ? -49.574 44.042 25.059  1.00 34.00 ? 324 THR   A OG1  1 
ATOM   2120 C  CG2  . THR   A 1 293 ? -50.325 45.964 26.349  1.00 33.74 ? 324 THR   A CG2  1 
ATOM   2121 N  N    . ILE   A 1 294 ? -46.999 45.808 28.266  1.00 32.02 ? 325 ILE   A N    1 
ATOM   2122 C  CA   . ILE   A 1 294 ? -46.569 46.639 29.398  1.00 34.90 ? 325 ILE   A CA   1 
ATOM   2123 C  C    . ILE   A 1 294 ? -45.299 47.416 29.041  1.00 37.79 ? 325 ILE   A C    1 
ATOM   2124 O  O    . ILE   A 1 294 ? -45.130 48.574 29.454  1.00 38.73 ? 325 ILE   A O    1 
ATOM   2125 C  CB   . ILE   A 1 294 ? -46.421 45.788 30.680  1.00 32.66 ? 325 ILE   A CB   1 
ATOM   2126 C  CG1  . ILE   A 1 294 ? -46.148 46.692 31.891  1.00 40.60 ? 325 ILE   A CG1  1 
ATOM   2127 C  CG2  . ILE   A 1 294 ? -45.337 44.722 30.560  1.00 35.23 ? 325 ILE   A CG2  1 
ATOM   2128 C  CD1  . ILE   A 1 294 ? -47.158 47.827 32.046  1.00 33.96 ? 325 ILE   A CD1  1 
ATOM   2129 N  N    . ILE   A 1 295 ? -44.419 46.828 28.220  1.00 37.19 ? 326 ILE   A N    1 
ATOM   2130 C  CA   . ILE   A 1 295 ? -43.271 47.565 27.690  1.00 37.81 ? 326 ILE   A CA   1 
ATOM   2131 C  C    . ILE   A 1 295 ? -43.734 48.758 26.856  1.00 39.05 ? 326 ILE   A C    1 
ATOM   2132 O  O    . ILE   A 1 295 ? -43.183 49.858 26.964  1.00 44.54 ? 326 ILE   A O    1 
ATOM   2133 C  CB   . ILE   A 1 295 ? -42.366 46.615 26.883  1.00 39.73 ? 326 ILE   A CB   1 
ATOM   2134 C  CG1  . ILE   A 1 295 ? -41.612 45.669 27.822  1.00 37.05 ? 326 ILE   A CG1  1 
ATOM   2135 C  CG2  . ILE   A 1 295 ? -41.394 47.388 25.991  1.00 39.73 ? 326 ILE   A CG2  1 
ATOM   2136 C  CD1  . ILE   A 1 295 ? -40.864 44.571 27.066  1.00 37.69 ? 326 ILE   A CD1  1 
ATOM   2137 N  N    . ALA   A 1 296 ? -44.753 48.568 26.016  1.00 39.12 ? 327 ALA   A N    1 
ATOM   2138 C  CA   . ALA   A 1 296 ? -45.256 49.687 25.218  1.00 38.37 ? 327 ALA   A CA   1 
ATOM   2139 C  C    . ALA   A 1 296 ? -45.913 50.747 26.097  1.00 41.08 ? 327 ALA   A C    1 
ATOM   2140 O  O    . ALA   A 1 296 ? -45.774 51.949 25.836  1.00 43.06 ? 327 ALA   A O    1 
ATOM   2141 C  CB   . ALA   A 1 296 ? -46.238 49.188 24.160  1.00 36.54 ? 327 ALA   A CB   1 
ATOM   2142 N  N    . ALA   A 1 297 ? -46.648 50.321 27.130  1.00 40.28 ? 328 ALA   A N    1 
ATOM   2143 C  CA   . ALA   A 1 297 ? -47.306 51.277 28.018  1.00 42.60 ? 328 ALA   A CA   1 
ATOM   2144 C  C    . ALA   A 1 297 ? -46.301 52.149 28.767  1.00 44.84 ? 328 ALA   A C    1 
ATOM   2145 O  O    . ALA   A 1 297 ? -46.584 53.320 29.046  1.00 48.66 ? 328 ALA   A O    1 
ATOM   2146 C  CB   . ALA   A 1 297 ? -48.218 50.540 29.002  1.00 36.18 ? 328 ALA   A CB   1 
ATOM   2147 N  N    . LYS   A 1 298 ? -45.123 51.613 29.084  1.00 41.52 ? 329 LYS   A N    1 
ATOM   2148 C  CA   . LYS   A 1 298 ? -44.097 52.380 29.780  1.00 45.26 ? 329 LYS   A CA   1 
ATOM   2149 C  C    . LYS   A 1 298 ? -43.267 53.269 28.866  1.00 54.25 ? 329 LYS   A C    1 
ATOM   2150 O  O    . LYS   A 1 298 ? -42.426 54.016 29.370  1.00 58.79 ? 329 LYS   A O    1 
ATOM   2151 C  CB   . LYS   A 1 298 ? -43.165 51.440 30.531  1.00 45.81 ? 329 LYS   A CB   1 
ATOM   2152 C  CG   . LYS   A 1 298 ? -43.857 50.660 31.609  1.00 44.16 ? 329 LYS   A CG   1 
ATOM   2153 C  CD   . LYS   A 1 298 ? -42.887 49.750 32.318  1.00 46.18 ? 329 LYS   A CD   1 
ATOM   2154 C  CE   . LYS   A 1 298 ? -43.509 49.217 33.580  1.00 44.38 ? 329 LYS   A CE   1 
ATOM   2155 N  NZ   . LYS   A 1 298 ? -42.501 48.560 34.447  1.00 53.10 ? 329 LYS   A NZ   1 
ATOM   2156 N  N    . LYS   A 1 299 ? -43.475 53.215 27.552  1.00 54.00 ? 330 LYS   A N    1 
ATOM   2157 C  CA   . LYS   A 1 299 ? -42.681 53.991 26.597  1.00 60.52 ? 330 LYS   A CA   1 
ATOM   2158 C  C    . LYS   A 1 299 ? -41.189 53.732 26.800  1.00 65.30 ? 330 LYS   A C    1 
ATOM   2159 O  O    . LYS   A 1 299 ? -40.367 54.651 26.835  1.00 67.52 ? 330 LYS   A O    1 
ATOM   2160 C  CB   . LYS   A 1 299 ? -43.000 55.484 26.699  1.00 58.94 ? 330 LYS   A CB   1 
ATOM   2161 C  CG   . LYS   A 1 299 ? -44.057 55.950 25.718  1.00 63.22 ? 330 LYS   A CG   1 
ATOM   2162 C  CD   . LYS   A 1 299 ? -45.467 55.866 26.279  1.00 64.52 ? 330 LYS   A CD   1 
ATOM   2163 C  CE   . LYS   A 1 299 ? -45.711 56.958 27.300  1.00 63.87 ? 330 LYS   A CE   1 
ATOM   2164 N  NZ   . LYS   A 1 299 ? -47.122 56.966 27.756  1.00 66.90 ? 330 LYS   A NZ   1 
ATOM   2165 N  N    . VAL   A 1 300 ? -40.853 52.446 26.941  1.00 62.65 ? 331 VAL   A N    1 
ATOM   2166 C  CA   . VAL   A 1 300 ? -39.480 52.024 27.214  1.00 63.60 ? 331 VAL   A CA   1 
ATOM   2167 C  C    . VAL   A 1 300 ? -38.548 52.391 26.062  1.00 67.69 ? 331 VAL   A C    1 
ATOM   2168 O  O    . VAL   A 1 300 ? -37.437 52.888 26.280  1.00 70.44 ? 331 VAL   A O    1 
ATOM   2169 C  CB   . VAL   A 1 300 ? -39.445 50.512 27.506  1.00 62.01 ? 331 VAL   A CB   1 
ATOM   2170 C  CG1  . VAL   A 1 300 ? -38.017 49.988 27.476  1.00 60.18 ? 331 VAL   A CG1  1 
ATOM   2171 C  CG2  . VAL   A 1 300 ? -40.113 50.212 28.848  1.00 60.81 ? 331 VAL   A CG2  1 
ATOM   2172 N  N    . LEU   A 1 301 ? -38.967 52.149 24.825  1.00 65.93 ? 332 LEU   A N    1 
ATOM   2173 C  CA   . LEU   A 1 301 ? -38.071 52.421 23.706  1.00 64.91 ? 332 LEU   A CA   1 
ATOM   2174 C  C    . LEU   A 1 301 ? -38.656 53.452 22.742  1.00 70.56 ? 332 LEU   A C    1 
ATOM   2175 O  O    . LEU   A 1 301 ? -38.599 54.659 22.999  1.00 69.68 ? 332 LEU   A O    1 
ATOM   2176 C  CB   . LEU   A 1 301 ? -37.727 51.113 22.978  1.00 67.50 ? 332 LEU   A CB   1 
ATOM   2177 C  CG   . LEU   A 1 301 ? -38.842 50.116 22.638  1.00 64.62 ? 332 LEU   A CG   1 
ATOM   2178 C  CD1  . LEU   A 1 301 ? -39.498 50.478 21.315  1.00 66.98 ? 332 LEU   A CD1  1 
ATOM   2179 C  CD2  . LEU   A 1 301 ? -38.321 48.686 22.607  1.00 53.62 ? 332 LEU   A CD2  1 
ATOM   2180 N  N    . GLU   B 1 5   ? -10.059 20.800 -12.342 1.00 74.09 ? 36  GLU   B N    1 
ATOM   2181 C  CA   . GLU   B 1 5   ? -9.585  22.016 -11.681 1.00 78.02 ? 36  GLU   B CA   1 
ATOM   2182 C  C    . GLU   B 1 5   ? -10.644 23.126 -11.801 1.00 73.64 ? 36  GLU   B C    1 
ATOM   2183 O  O    . GLU   B 1 5   ? -11.433 23.140 -12.749 1.00 66.55 ? 36  GLU   B O    1 
ATOM   2184 C  CB   . GLU   B 1 5   ? -8.243  22.455 -12.277 1.00 77.36 ? 36  GLU   B CB   1 
ATOM   2185 C  CG   . GLU   B 1 5   ? -7.403  23.370 -11.385 1.00 81.39 ? 36  GLU   B CG   1 
ATOM   2186 C  CD   . GLU   B 1 5   ? -5.957  23.498 -11.868 1.00 86.70 ? 36  GLU   B CD   1 
ATOM   2187 O  OE1  . GLU   B 1 5   ? -5.321  22.453 -12.132 1.00 87.90 ? 36  GLU   B OE1  1 
ATOM   2188 O  OE2  . GLU   B 1 5   ? -5.457  24.642 -11.986 1.00 86.04 ? 36  GLU   B OE2  1 
ATOM   2189 N  N    . ALA   B 1 6   ? -10.660 24.048 -10.834 1.00 73.78 ? 37  ALA   B N    1 
ATOM   2190 C  CA   . ALA   B 1 6   ? -11.774 24.982 -10.679 1.00 67.92 ? 37  ALA   B CA   1 
ATOM   2191 C  C    . ALA   B 1 6   ? -11.757 26.095 -11.726 1.00 62.85 ? 37  ALA   B C    1 
ATOM   2192 O  O    . ALA   B 1 6   ? -10.717 26.717 -11.974 1.00 64.70 ? 37  ALA   B O    1 
ATOM   2193 C  CB   . ALA   B 1 6   ? -11.750 25.602 -9.283  1.00 60.70 ? 37  ALA   B CB   1 
ATOM   2194 N  N    . VAL   B 1 7   ? -12.923 26.358 -12.324 1.00 53.06 ? 38  VAL   B N    1 
ATOM   2195 C  CA   . VAL   B 1 7   ? -13.137 27.630 -12.998 1.00 56.39 ? 38  VAL   B CA   1 
ATOM   2196 C  C    . VAL   B 1 7   ? -12.861 28.762 -12.019 1.00 57.51 ? 38  VAL   B C    1 
ATOM   2197 O  O    . VAL   B 1 7   ? -13.418 28.786 -10.917 1.00 56.27 ? 38  VAL   B O    1 
ATOM   2198 C  CB   . VAL   B 1 7   ? -14.576 27.710 -13.537 1.00 55.98 ? 38  VAL   B CB   1 
ATOM   2199 C  CG1  . VAL   B 1 7   ? -14.838 29.088 -14.130 1.00 54.82 ? 38  VAL   B CG1  1 
ATOM   2200 C  CG2  . VAL   B 1 7   ? -14.840 26.608 -14.552 1.00 56.94 ? 38  VAL   B CG2  1 
ATOM   2201 N  N    . VAL   B 1 8   ? -11.999 29.699 -12.404 1.00 56.84 ? 39  VAL   B N    1 
ATOM   2202 C  CA   . VAL   B 1 8   ? -11.709 30.870 -11.583 1.00 51.32 ? 39  VAL   B CA   1 
ATOM   2203 C  C    . VAL   B 1 8   ? -12.578 32.008 -12.095 1.00 56.06 ? 39  VAL   B C    1 
ATOM   2204 O  O    . VAL   B 1 8   ? -12.336 32.547 -13.180 1.00 48.46 ? 39  VAL   B O    1 
ATOM   2205 C  CB   . VAL   B 1 8   ? -10.224 31.247 -11.606 1.00 54.38 ? 39  VAL   B CB   1 
ATOM   2206 C  CG1  . VAL   B 1 8   ? -10.032 32.674 -11.079 1.00 51.20 ? 39  VAL   B CG1  1 
ATOM   2207 C  CG2  . VAL   B 1 8   ? -9.426  30.276 -10.759 1.00 57.61 ? 39  VAL   B CG2  1 
ATOM   2208 N  N    . ILE   B 1 9   ? -13.605 32.368 -11.322 1.00 52.00 ? 40  ILE   B N    1 
ATOM   2209 C  CA   . ILE   B 1 9   ? -14.505 33.434 -11.739 1.00 51.43 ? 40  ILE   B CA   1 
ATOM   2210 C  C    . ILE   B 1 9   ? -13.761 34.757 -11.680 1.00 47.30 ? 40  ILE   B C    1 
ATOM   2211 O  O    . ILE   B 1 9   ? -13.093 35.070 -10.687 1.00 52.25 ? 40  ILE   B O    1 
ATOM   2212 C  CB   . ILE   B 1 9   ? -15.761 33.463 -10.857 1.00 49.66 ? 40  ILE   B CB   1 
ATOM   2213 C  CG1  . ILE   B 1 9   ? -16.527 32.147 -10.954 1.00 50.26 ? 40  ILE   B CG1  1 
ATOM   2214 C  CG2  . ILE   B 1 9   ? -16.670 34.608 -11.268 1.00 46.81 ? 40  ILE   B CG2  1 
ATOM   2215 C  CD1  . ILE   B 1 9   ? -17.658 32.052 -9.939  1.00 50.22 ? 40  ILE   B CD1  1 
ATOM   2216 N  N    . SER   B 1 10  ? -13.871 35.542 -12.737 1.00 44.98 ? 41  SER   B N    1 
ATOM   2217 C  CA   . SER   B 1 10  ? -13.235 36.851 -12.780 1.00 48.54 ? 41  SER   B CA   1 
ATOM   2218 C  C    . SER   B 1 10  ? -14.249 37.898 -12.329 1.00 44.20 ? 41  SER   B C    1 
ATOM   2219 O  O    . SER   B 1 10  ? -15.211 38.194 -13.050 1.00 41.27 ? 41  SER   B O    1 
ATOM   2220 C  CB   . SER   B 1 10  ? -12.714 37.159 -14.182 1.00 47.51 ? 41  SER   B CB   1 
ATOM   2221 O  OG   . SER   B 1 10  ? -12.186 38.469 -14.206 1.00 49.75 ? 41  SER   B OG   1 
ATOM   2222 N  N    . GLY   B 1 11  ? -14.047 38.437 -11.121 1.00 45.88 ? 42  GLY   B N    1 
ATOM   2223 C  CA   . GLY   B 1 11  ? -14.860 39.555 -10.678 1.00 43.05 ? 42  GLY   B CA   1 
ATOM   2224 C  C    . GLY   B 1 11  ? -14.607 40.811 -11.486 1.00 44.47 ? 42  GLY   B C    1 
ATOM   2225 O  O    . GLY   B 1 11  ? -15.503 41.645 -11.644 1.00 43.05 ? 42  GLY   B O    1 
ATOM   2226 N  N    . ARG   B 1 12  ? -13.393 40.959 -12.020 1.00 42.80 ? 43  ARG   B N    1 
ATOM   2227 C  CA   . ARG   B 1 12  ? -13.093 42.105 -12.865 1.00 44.65 ? 43  ARG   B CA   1 
ATOM   2228 C  C    . ARG   B 1 12  ? -13.911 42.073 -14.150 1.00 43.58 ? 43  ARG   B C    1 
ATOM   2229 O  O    . ARG   B 1 12  ? -14.509 43.083 -14.535 1.00 42.95 ? 43  ARG   B O    1 
ATOM   2230 C  CB   . ARG   B 1 12  ? -11.600 42.150 -13.164 1.00 45.07 ? 43  ARG   B CB   1 
ATOM   2231 C  CG   . ARG   B 1 12  ? -10.791 42.723 -12.029 1.00 45.72 ? 43  ARG   B CG   1 
ATOM   2232 C  CD   . ARG   B 1 12  ? -9.348  42.877 -12.446 1.00 52.25 ? 43  ARG   B CD   1 
ATOM   2233 N  NE   . ARG   B 1 12  ? -8.520  41.748 -12.041 1.00 59.18 ? 43  ARG   B NE   1 
ATOM   2234 C  CZ   . ARG   B 1 12  ? -7.754  41.730 -10.953 1.00 62.56 ? 43  ARG   B CZ   1 
ATOM   2235 N  NH1  . ARG   B 1 12  ? -7.012  40.675 -10.645 1.00 63.38 ? 43  ARG   B NH1  1 
ATOM   2236 N  NH2  . ARG   B 1 12  ? -7.727  42.798 -10.157 1.00 56.67 ? 43  ARG   B NH2  1 
ATOM   2237 N  N    . LYS   B 1 13  ? -13.977 40.914 -14.815 1.00 44.64 ? 44  LYS   B N    1 
ATOM   2238 C  CA   . LYS   B 1 13  ? -14.757 40.829 -16.049 1.00 44.78 ? 44  LYS   B CA   1 
ATOM   2239 C  C    . LYS   B 1 13  ? -16.249 41.000 -15.782 1.00 43.87 ? 44  LYS   B C    1 
ATOM   2240 O  O    . LYS   B 1 13  ? -16.943 41.673 -16.549 1.00 39.19 ? 44  LYS   B O    1 
ATOM   2241 C  CB   . LYS   B 1 13  ? -14.491 39.506 -16.765 1.00 48.72 ? 44  LYS   B CB   1 
ATOM   2242 C  CG   . LYS   B 1 13  ? -13.633 39.619 -18.026 1.00 61.28 ? 44  LYS   B CG   1 
ATOM   2243 C  CD   . LYS   B 1 13  ? -12.146 39.761 -17.708 1.00 66.13 ? 44  LYS   B CD   1 
ATOM   2244 C  CE   . LYS   B 1 13  ? -11.312 39.899 -18.987 1.00 64.91 ? 44  LYS   B CE   1 
ATOM   2245 N  NZ   . LYS   B 1 13  ? -11.686 38.880 -20.017 1.00 72.30 ? 44  LYS   B NZ   1 
ATOM   2246 N  N    . LEU   B 1 14  ? -16.766 40.407 -14.699 1.00 40.78 ? 45  LEU   B N    1 
ATOM   2247 C  CA   . LEU   B 1 14  ? -18.187 40.577 -14.407 1.00 39.93 ? 45  LEU   B CA   1 
ATOM   2248 C  C    . LEU   B 1 14  ? -18.515 42.033 -14.085 1.00 35.33 ? 45  LEU   B C    1 
ATOM   2249 O  O    . LEU   B 1 14  ? -19.567 42.545 -14.486 1.00 38.11 ? 45  LEU   B O    1 
ATOM   2250 C  CB   . LEU   B 1 14  ? -18.613 39.653 -13.259 1.00 41.60 ? 45  LEU   B CB   1 
ATOM   2251 C  CG   . LEU   B 1 14  ? -18.749 38.166 -13.609 1.00 45.58 ? 45  LEU   B CG   1 
ATOM   2252 C  CD1  . LEU   B 1 14  ? -19.205 37.364 -12.396 1.00 44.86 ? 45  LEU   B CD1  1 
ATOM   2253 C  CD2  . LEU   B 1 14  ? -19.714 37.959 -14.775 1.00 43.12 ? 45  LEU   B CD2  1 
ATOM   2254 N  N    . ALA   B 1 15  ? -17.633 42.719 -13.360 1.00 37.34 ? 46  ALA   B N    1 
ATOM   2255 C  CA   . ALA   B 1 15  ? -17.926 44.102 -12.993 1.00 40.92 ? 46  ALA   B CA   1 
ATOM   2256 C  C    . ALA   B 1 15  ? -17.845 45.023 -14.199 1.00 39.53 ? 46  ALA   B C    1 
ATOM   2257 O  O    . ALA   B 1 15  ? -18.604 45.996 -14.302 1.00 39.01 ? 46  ALA   B O    1 
ATOM   2258 C  CB   . ALA   B 1 15  ? -16.972 44.572 -11.900 1.00 37.29 ? 46  ALA   B CB   1 
ATOM   2259 N  N    . GLN   B 1 16  ? -16.923 44.736 -15.110 1.00 39.78 ? 47  GLN   B N    1 
ATOM   2260 C  CA   . GLN   B 1 16  ? -16.872 45.447 -16.377 1.00 38.80 ? 47  GLN   B CA   1 
ATOM   2261 C  C    . GLN   B 1 16  ? -18.219 45.388 -17.088 1.00 37.64 ? 47  GLN   B C    1 
ATOM   2262 O  O    . GLN   B 1 16  ? -18.743 46.415 -17.529 1.00 41.69 ? 47  GLN   B O    1 
ATOM   2263 C  CB   . GLN   B 1 16  ? -15.747 44.836 -17.206 1.00 42.44 ? 47  GLN   B CB   1 
ATOM   2264 C  CG   . GLN   B 1 16  ? -15.487 45.404 -18.578 1.00 47.08 ? 47  GLN   B CG   1 
ATOM   2265 C  CD   . GLN   B 1 16  ? -14.490 44.519 -19.297 1.00 50.28 ? 47  GLN   B CD   1 
ATOM   2266 O  OE1  . GLN   B 1 16  ? -13.284 44.588 -19.039 1.00 54.40 ? 47  GLN   B OE1  1 
ATOM   2267 N  NE2  . GLN   B 1 16  ? -14.995 43.626 -20.145 1.00 52.10 ? 47  GLN   B NE2  1 
ATOM   2268 N  N    . GLN   B 1 17  ? -18.832 44.203 -17.152 1.00 40.12 ? 48  GLN   B N    1 
ATOM   2269 C  CA   . GLN   B 1 17  ? -20.160 44.095 -17.764 1.00 42.95 ? 48  GLN   B CA   1 
ATOM   2270 C  C    . GLN   B 1 17  ? -21.187 44.927 -17.007 1.00 40.41 ? 48  GLN   B C    1 
ATOM   2271 O  O    . GLN   B 1 17  ? -21.965 45.675 -17.608 1.00 42.72 ? 48  GLN   B O    1 
ATOM   2272 C  CB   . GLN   B 1 17  ? -20.621 42.639 -17.802 1.00 47.04 ? 48  GLN   B CB   1 
ATOM   2273 C  CG   . GLN   B 1 17  ? -19.767 41.711 -18.625 1.00 57.60 ? 48  GLN   B CG   1 
ATOM   2274 C  CD   . GLN   B 1 17  ? -20.338 40.307 -18.644 1.00 65.88 ? 48  GLN   B CD   1 
ATOM   2275 O  OE1  . GLN   B 1 17  ? -21.366 40.034 -18.009 1.00 70.18 ? 48  GLN   B OE1  1 
ATOM   2276 N  NE2  . GLN   B 1 17  ? -19.677 39.405 -19.370 1.00 67.18 ? 48  GLN   B NE2  1 
ATOM   2277 N  N    . ILE   B 1 18  ? -21.206 44.804 -15.677 1.00 41.40 ? 49  ILE   B N    1 
ATOM   2278 C  CA   . ILE   B 1 18  ? -22.176 45.558 -14.886 1.00 42.26 ? 49  ILE   B CA   1 
ATOM   2279 C  C    . ILE   B 1 18  ? -21.975 47.056 -15.085 1.00 37.42 ? 49  ILE   B C    1 
ATOM   2280 O  O    . ILE   B 1 18  ? -22.938 47.808 -15.274 1.00 37.84 ? 49  ILE   B O    1 
ATOM   2281 C  CB   . ILE   B 1 18  ? -22.081 45.155 -13.403 1.00 40.88 ? 49  ILE   B CB   1 
ATOM   2282 C  CG1  . ILE   B 1 18  ? -22.754 43.799 -13.198 1.00 42.10 ? 49  ILE   B CG1  1 
ATOM   2283 C  CG2  . ILE   B 1 18  ? -22.723 46.228 -12.508 1.00 40.45 ? 49  ILE   B CG2  1 
ATOM   2284 C  CD1  . ILE   B 1 18  ? -22.146 42.977 -12.126 1.00 46.74 ? 49  ILE   B CD1  1 
ATOM   2285 N  N    . LYS   B 1 19  ? -20.721 47.510 -15.077 1.00 38.40 ? 50  LYS   B N    1 
ATOM   2286 C  CA   . LYS   B 1 19  ? -20.461 48.934 -15.260 1.00 37.53 ? 50  LYS   B CA   1 
ATOM   2287 C  C    . LYS   B 1 19  ? -20.870 49.398 -16.656 1.00 39.07 ? 50  LYS   B C    1 
ATOM   2288 O  O    . LYS   B 1 19  ? -21.379 50.512 -16.826 1.00 39.45 ? 50  LYS   B O    1 
ATOM   2289 C  CB   . LYS   B 1 19  ? -18.987 49.229 -14.979 1.00 37.76 ? 50  LYS   B CB   1 
ATOM   2290 C  CG   . LYS   B 1 19  ? -18.654 49.193 -13.503 1.00 38.86 ? 50  LYS   B CG   1 
ATOM   2291 C  CD   . LYS   B 1 19  ? -17.210 49.578 -13.226 1.00 40.82 ? 50  LYS   B CD   1 
ATOM   2292 C  CE   . LYS   B 1 19  ? -16.267 48.419 -13.498 1.00 38.75 ? 50  LYS   B CE   1 
ATOM   2293 N  NZ   . LYS   B 1 19  ? -14.925 48.689 -12.919 1.00 38.84 ? 50  LYS   B NZ   1 
ATOM   2294 N  N    . GLN   B 1 20  ? -20.680 48.557 -17.667 1.00 39.67 ? 51  GLN   B N    1 
ATOM   2295 C  CA   . GLN   B 1 20  ? -21.129 48.948 -18.998 1.00 44.51 ? 51  GLN   B CA   1 
ATOM   2296 C  C    . GLN   B 1 20  ? -22.649 49.060 -19.045 1.00 42.09 ? 51  GLN   B C    1 
ATOM   2297 O  O    . GLN   B 1 20  ? -23.189 49.994 -19.649 1.00 41.93 ? 51  GLN   B O    1 
ATOM   2298 C  CB   . GLN   B 1 20  ? -20.606 47.967 -20.049 1.00 43.89 ? 51  GLN   B CB   1 
ATOM   2299 C  CG   . GLN   B 1 20  ? -21.037 48.313 -21.469 1.00 49.39 ? 51  GLN   B CG   1 
ATOM   2300 C  CD   . GLN   B 1 20  ? -20.954 49.814 -21.772 1.00 55.64 ? 51  GLN   B CD   1 
ATOM   2301 O  OE1  . GLN   B 1 20  ? -21.953 50.432 -22.158 1.00 54.11 ? 51  GLN   B OE1  1 
ATOM   2302 N  NE2  . GLN   B 1 20  ? -19.764 50.402 -21.598 1.00 51.33 ? 51  GLN   B NE2  1 
ATOM   2303 N  N    . GLU   B 1 21  ? -23.358 48.136 -18.383 1.00 41.10 ? 52  GLU   B N    1 
ATOM   2304 C  CA   . GLU   B 1 21  ? -24.808 48.271 -18.287 1.00 42.79 ? 52  GLU   B CA   1 
ATOM   2305 C  C    . GLU   B 1 21  ? -25.193 49.584 -17.626 1.00 42.58 ? 52  GLU   B C    1 
ATOM   2306 O  O    . GLU   B 1 21  ? -26.128 50.255 -18.070 1.00 41.86 ? 52  GLU   B O    1 
ATOM   2307 C  CB   . GLU   B 1 21  ? -25.408 47.111 -17.500 1.00 41.97 ? 52  GLU   B CB   1 
ATOM   2308 C  CG   . GLU   B 1 21  ? -25.292 45.771 -18.162 1.00 44.61 ? 52  GLU   B CG   1 
ATOM   2309 C  CD   . GLU   B 1 21  ? -25.705 44.649 -17.235 1.00 46.05 ? 52  GLU   B CD   1 
ATOM   2310 O  OE1  . GLU   B 1 21  ? -26.185 44.937 -16.107 1.00 45.51 ? 52  GLU   B OE1  1 
ATOM   2311 O  OE2  . GLU   B 1 21  ? -25.534 43.480 -17.622 1.00 44.81 ? 52  GLU   B OE2  1 
ATOM   2312 N  N    . VAL   B 1 22  ? -24.486 49.967 -16.558 1.00 41.26 ? 53  VAL   B N    1 
ATOM   2313 C  CA   . VAL   B 1 22  ? -24.807 51.216 -15.872 1.00 38.74 ? 53  VAL   B CA   1 
ATOM   2314 C  C    . VAL   B 1 22  ? -24.506 52.429 -16.753 1.00 34.59 ? 53  VAL   B C    1 
ATOM   2315 O  O    . VAL   B 1 22  ? -25.297 53.375 -16.810 1.00 36.46 ? 53  VAL   B O    1 
ATOM   2316 C  CB   . VAL   B 1 22  ? -24.066 51.286 -14.528 1.00 35.82 ? 53  VAL   B CB   1 
ATOM   2317 C  CG1  . VAL   B 1 22  ? -24.215 52.677 -13.914 1.00 31.97 ? 53  VAL   B CG1  1 
ATOM   2318 C  CG2  . VAL   B 1 22  ? -24.604 50.216 -13.598 1.00 40.43 ? 53  VAL   B CG2  1 
ATOM   2319 N  N    . ARG   B 1 23  ? -23.364 52.435 -17.444 1.00 37.94 ? 54  ARG   B N    1 
ATOM   2320 C  CA   . ARG   B 1 23  ? -23.059 53.559 -18.333 1.00 37.88 ? 54  ARG   B CA   1 
ATOM   2321 C  C    . ARG   B 1 23  ? -24.153 53.747 -19.382 1.00 39.08 ? 54  ARG   B C    1 
ATOM   2322 O  O    . ARG   B 1 23  ? -24.577 54.877 -19.665 1.00 37.82 ? 54  ARG   B O    1 
ATOM   2323 C  CB   . ARG   B 1 23  ? -21.706 53.348 -19.011 1.00 39.48 ? 54  ARG   B CB   1 
ATOM   2324 C  CG   . ARG   B 1 23  ? -21.502 54.315 -20.172 1.00 40.30 ? 54  ARG   B CG   1 
ATOM   2325 C  CD   . ARG   B 1 23  ? -20.054 54.722 -20.342 1.00 50.79 ? 54  ARG   B CD   1 
ATOM   2326 N  NE   . ARG   B 1 23  ? -19.338 53.758 -21.165 1.00 55.36 ? 54  ARG   B NE   1 
ATOM   2327 C  CZ   . ARG   B 1 23  ? -18.418 54.080 -22.067 1.00 61.35 ? 54  ARG   B CZ   1 
ATOM   2328 N  NH1  . ARG   B 1 23  ? -18.004 55.329 -22.222 1.00 54.90 ? 54  ARG   B NH1  1 
ATOM   2329 N  NH2  . ARG   B 1 23  ? -17.915 53.127 -22.847 1.00 54.80 ? 54  ARG   B NH2  1 
ATOM   2330 N  N    . GLN   B 1 24  ? -24.639 52.643 -19.943 1.00 39.54 ? 55  GLN   B N    1 
ATOM   2331 C  CA   . GLN   B 1 24  ? -25.745 52.701 -20.896 1.00 44.37 ? 55  GLN   B CA   1 
ATOM   2332 C  C    . GLN   B 1 24  ? -27.006 53.253 -20.245 1.00 43.25 ? 55  GLN   B C    1 
ATOM   2333 O  O    . GLN   B 1 24  ? -27.664 54.149 -20.793 1.00 38.27 ? 55  GLN   B O    1 
ATOM   2334 C  CB   . GLN   B 1 24  ? -25.993 51.296 -21.432 1.00 48.50 ? 55  GLN   B CB   1 
ATOM   2335 C  CG   . GLN   B 1 24  ? -26.592 51.224 -22.794 1.00 59.10 ? 55  GLN   B CG   1 
ATOM   2336 C  CD   . GLN   B 1 24  ? -26.200 49.938 -23.480 1.00 66.90 ? 55  GLN   B CD   1 
ATOM   2337 O  OE1  . GLN   B 1 24  ? -25.243 49.905 -24.261 1.00 72.50 ? 55  GLN   B OE1  1 
ATOM   2338 N  NE2  . GLN   B 1 24  ? -26.921 48.862 -23.180 1.00 71.09 ? 55  GLN   B NE2  1 
ATOM   2339 N  N    . GLU   B 1 25  ? -27.343 52.741 -19.059 1.00 42.08 ? 56  GLU   B N    1 
ATOM   2340 C  CA   . GLU   B 1 25  ? -28.532 53.216 -18.363 1.00 39.61 ? 56  GLU   B CA   1 
ATOM   2341 C  C    . GLU   B 1 25  ? -28.411 54.700 -18.029 1.00 40.02 ? 56  GLU   B C    1 
ATOM   2342 O  O    . GLU   B 1 25  ? -29.371 55.461 -18.189 1.00 42.04 ? 56  GLU   B O    1 
ATOM   2343 C  CB   . GLU   B 1 25  ? -28.759 52.378 -17.094 1.00 41.19 ? 56  GLU   B CB   1 
ATOM   2344 C  CG   . GLU   B 1 25  ? -29.948 52.853 -16.281 1.00 42.16 ? 56  GLU   B CG   1 
ATOM   2345 C  CD   . GLU   B 1 25  ? -30.314 51.950 -15.112 1.00 46.68 ? 56  GLU   B CD   1 
ATOM   2346 O  OE1  . GLU   B 1 25  ? -29.549 51.010 -14.787 1.00 46.83 ? 56  GLU   B OE1  1 
ATOM   2347 O  OE2  . GLU   B 1 25  ? -31.384 52.197 -14.514 1.00 44.15 ? 56  GLU   B OE2  1 
ATOM   2348 N  N    . VAL   B 1 26  ? -27.233 55.132 -17.570 1.00 38.28 ? 57  VAL   B N    1 
ATOM   2349 C  CA   . VAL   B 1 26  ? -27.046 56.537 -17.218 1.00 41.25 ? 57  VAL   B CA   1 
ATOM   2350 C  C    . VAL   B 1 26  ? -27.124 57.417 -18.463 1.00 41.20 ? 57  VAL   B C    1 
ATOM   2351 O  O    . VAL   B 1 26  ? -27.711 58.508 -18.438 1.00 41.65 ? 57  VAL   B O    1 
ATOM   2352 C  CB   . VAL   B 1 26  ? -25.714 56.731 -16.460 1.00 40.87 ? 57  VAL   B CB   1 
ATOM   2353 C  CG1  . VAL   B 1 26  ? -25.307 58.206 -16.444 1.00 38.69 ? 57  VAL   B CG1  1 
ATOM   2354 C  CG2  . VAL   B 1 26  ? -25.814 56.174 -15.011 1.00 34.64 ? 57  VAL   B CG2  1 
ATOM   2355 N  N    . GLU   B 1 27  ? -26.534 56.969 -19.568 1.00 42.69 ? 58  GLU   B N    1 
ATOM   2356 C  CA   . GLU   B 1 27  ? -26.551 57.804 -20.766 1.00 47.71 ? 58  GLU   B CA   1 
ATOM   2357 C  C    . GLU   B 1 27  ? -27.959 57.917 -21.353 1.00 44.83 ? 58  GLU   B C    1 
ATOM   2358 O  O    . GLU   B 1 27  ? -28.363 59.004 -21.779 1.00 47.66 ? 58  GLU   B O    1 
ATOM   2359 C  CB   . GLU   B 1 27  ? -25.548 57.279 -21.799 1.00 48.36 ? 58  GLU   B CB   1 
ATOM   2360 C  CG   . GLU   B 1 27  ? -24.786 58.404 -22.511 1.00 60.65 ? 58  GLU   B CG   1 
ATOM   2361 C  CD   . GLU   B 1 27  ? -24.308 59.512 -21.547 1.00 68.33 ? 58  GLU   B CD   1 
ATOM   2362 O  OE1  . GLU   B 1 27  ? -23.451 59.246 -20.650 1.00 65.15 ? 58  GLU   B OE1  1 
ATOM   2363 O  OE2  . GLU   B 1 27  ? -24.809 60.657 -21.685 1.00 67.04 ? 58  GLU   B OE2  1 
ATOM   2364 N  N    . GLU   B 1 28  ? -28.737 56.825 -21.361 1.00 43.29 ? 59  GLU   B N    1 
ATOM   2365 C  CA   . GLU   B 1 28  ? -30.129 56.944 -21.807 1.00 46.53 ? 59  GLU   B CA   1 
ATOM   2366 C  C    . GLU   B 1 28  ? -30.896 57.905 -20.909 1.00 47.44 ? 59  GLU   B C    1 
ATOM   2367 O  O    . GLU   B 1 28  ? -31.655 58.757 -21.389 1.00 46.99 ? 59  GLU   B O    1 
ATOM   2368 C  CB   . GLU   B 1 28  ? -30.817 55.575 -21.829 1.00 47.92 ? 59  GLU   B CB   1 
ATOM   2369 C  CG   . GLU   B 1 28  ? -30.494 54.719 -23.053 1.00 58.70 ? 59  GLU   B CG   1 
ATOM   2370 C  CD   . GLU   B 1 28  ? -30.984 53.273 -22.933 1.00 65.59 ? 59  GLU   B CD   1 
ATOM   2371 O  OE1  . GLU   B 1 28  ? -30.186 52.335 -23.184 1.00 64.63 ? 59  GLU   B OE1  1 
ATOM   2372 O  OE2  . GLU   B 1 28  ? -32.176 53.080 -22.588 1.00 67.31 ? 59  GLU   B OE2  1 
ATOM   2373 N  N    . TRP   B 1 29  ? -30.662 57.806 -19.599 1.00 44.84 ? 60  TRP   B N    1 
ATOM   2374 C  CA   . TRP   B 1 29  ? -31.271 58.703 -18.623 1.00 43.60 ? 60  TRP   B CA   1 
ATOM   2375 C  C    . TRP   B 1 29  ? -30.916 60.157 -18.904 1.00 43.09 ? 60  TRP   B C    1 
ATOM   2376 O  O    . TRP   B 1 29  ? -31.793 61.025 -18.950 1.00 45.12 ? 60  TRP   B O    1 
ATOM   2377 C  CB   . TRP   B 1 29  ? -30.802 58.273 -17.228 1.00 46.19 ? 60  TRP   B CB   1 
ATOM   2378 C  CG   . TRP   B 1 29  ? -31.257 59.087 -16.074 1.00 44.61 ? 60  TRP   B CG   1 
ATOM   2379 C  CD1  . TRP   B 1 29  ? -30.484 59.888 -15.283 1.00 46.62 ? 60  TRP   B CD1  1 
ATOM   2380 C  CD2  . TRP   B 1 29  ? -32.585 59.150 -15.538 1.00 46.29 ? 60  TRP   B CD2  1 
ATOM   2381 N  NE1  . TRP   B 1 29  ? -31.252 60.460 -14.297 1.00 47.86 ? 60  TRP   B NE1  1 
ATOM   2382 C  CE2  . TRP   B 1 29  ? -32.545 60.022 -14.432 1.00 47.34 ? 60  TRP   B CE2  1 
ATOM   2383 C  CE3  . TRP   B 1 29  ? -33.807 58.569 -15.899 1.00 46.00 ? 60  TRP   B CE3  1 
ATOM   2384 C  CZ2  . TRP   B 1 29  ? -33.679 60.325 -13.678 1.00 46.24 ? 60  TRP   B CZ2  1 
ATOM   2385 C  CZ3  . TRP   B 1 29  ? -34.930 58.871 -15.151 1.00 47.75 ? 60  TRP   B CZ3  1 
ATOM   2386 C  CH2  . TRP   B 1 29  ? -34.856 59.737 -14.048 1.00 47.10 ? 60  TRP   B CH2  1 
ATOM   2387 N  N    . VAL   B 1 30  ? -29.630 60.446 -19.104 1.00 42.91 ? 61  VAL   B N    1 
ATOM   2388 C  CA   . VAL   B 1 30  ? -29.224 61.825 -19.361 1.00 42.94 ? 61  VAL   B CA   1 
ATOM   2389 C  C    . VAL   B 1 30  ? -29.716 62.275 -20.733 1.00 48.28 ? 61  VAL   B C    1 
ATOM   2390 O  O    . VAL   B 1 30  ? -30.156 63.418 -20.909 1.00 48.52 ? 61  VAL   B O    1 
ATOM   2391 C  CB   . VAL   B 1 30  ? -27.696 61.966 -19.213 1.00 47.32 ? 61  VAL   B CB   1 
ATOM   2392 C  CG1  . VAL   B 1 30  ? -27.205 63.271 -19.813 1.00 44.48 ? 61  VAL   B CG1  1 
ATOM   2393 C  CG2  . VAL   B 1 30  ? -27.295 61.886 -17.726 1.00 42.28 ? 61  VAL   B CG2  1 
ATOM   2394 N  N    . ALA   B 1 31  ? -29.679 61.373 -21.714 1.00 46.77 ? 62  ALA   B N    1 
ATOM   2395 C  CA   . ALA   B 1 31  ? -30.135 61.716 -23.058 1.00 49.70 ? 62  ALA   B CA   1 
ATOM   2396 C  C    . ALA   B 1 31  ? -31.590 62.150 -23.057 1.00 52.44 ? 62  ALA   B C    1 
ATOM   2397 O  O    . ALA   B 1 31  ? -31.990 62.977 -23.884 1.00 51.95 ? 62  ALA   B O    1 
ATOM   2398 C  CB   . ALA   B 1 31  ? -29.935 60.532 -23.999 1.00 44.97 ? 62  ALA   B CB   1 
ATOM   2399 N  N    . SER   B 1 32  ? -32.390 61.621 -22.130 1.00 50.17 ? 63  SER   B N    1 
ATOM   2400 C  CA   . SER   B 1 32  ? -33.803 61.951 -22.031 1.00 47.23 ? 63  SER   B CA   1 
ATOM   2401 C  C    . SER   B 1 32  ? -34.054 63.251 -21.285 1.00 49.83 ? 63  SER   B C    1 
ATOM   2402 O  O    . SER   B 1 32  ? -35.209 63.571 -20.986 1.00 50.47 ? 63  SER   B O    1 
ATOM   2403 C  CB   . SER   B 1 32  ? -34.556 60.805 -21.354 1.00 53.07 ? 63  SER   B CB   1 
ATOM   2404 O  OG   . SER   B 1 32  ? -34.434 59.620 -22.124 1.00 56.29 ? 63  SER   B OG   1 
ATOM   2405 N  N    . GLY   B 1 33  ? -33.008 64.000 -20.956 1.00 48.96 ? 64  GLY   B N    1 
ATOM   2406 C  CA   . GLY   B 1 33  ? -33.178 65.295 -20.335 1.00 45.49 ? 64  GLY   B CA   1 
ATOM   2407 C  C    . GLY   B 1 33  ? -33.084 65.336 -18.826 1.00 52.45 ? 64  GLY   B C    1 
ATOM   2408 O  O    . GLY   B 1 33  ? -33.287 66.410 -18.247 1.00 55.69 ? 64  GLY   B O    1 
ATOM   2409 N  N    . ASN   B 1 34  ? -32.772 64.226 -18.166 1.00 50.52 ? 65  ASN   B N    1 
ATOM   2410 C  CA   . ASN   B 1 34  ? -32.650 64.260 -16.715 1.00 50.64 ? 65  ASN   B CA   1 
ATOM   2411 C  C    . ASN   B 1 34  ? -31.254 64.702 -16.293 1.00 46.97 ? 65  ASN   B C    1 
ATOM   2412 O  O    . ASN   B 1 34  ? -30.283 64.595 -17.045 1.00 47.69 ? 65  ASN   B O    1 
ATOM   2413 C  CB   . ASN   B 1 34  ? -32.956 62.895 -16.103 1.00 47.87 ? 65  ASN   B CB   1 
ATOM   2414 C  CG   . ASN   B 1 34  ? -34.255 62.314 -16.589 1.00 49.68 ? 65  ASN   B CG   1 
ATOM   2415 O  OD1  . ASN   B 1 34  ? -35.331 62.637 -16.081 1.00 50.74 ? 65  ASN   B OD1  1 
ATOM   2416 N  ND2  . ASN   B 1 34  ? -34.164 61.435 -17.571 1.00 49.70 ? 65  ASN   B ND2  1 
ATOM   2417 N  N    . LYS   B 1 35  ? -31.169 65.171 -15.053 1.00 47.27 ? 66  LYS   B N    1 
ATOM   2418 C  CA   . LYS   B 1 35  ? -29.903 65.560 -14.445 1.00 45.99 ? 66  LYS   B CA   1 
ATOM   2419 C  C    . LYS   B 1 35  ? -28.935 64.380 -14.400 1.00 45.00 ? 66  LYS   B C    1 
ATOM   2420 O  O    . LYS   B 1 35  ? -29.333 63.237 -14.158 1.00 45.13 ? 66  LYS   B O    1 
ATOM   2421 C  CB   . LYS   B 1 35  ? -30.172 66.082 -13.029 1.00 48.94 ? 66  LYS   B CB   1 
ATOM   2422 C  CG   . LYS   B 1 35  ? -28.966 66.602 -12.263 1.00 47.51 ? 66  LYS   B CG   1 
ATOM   2423 C  CD   . LYS   B 1 35  ? -29.337 66.882 -10.794 1.00 52.80 ? 66  LYS   B CD   1 
ATOM   2424 C  CE   . LYS   B 1 35  ? -29.265 65.614 -9.933  1.00 47.77 ? 66  LYS   B CE   1 
ATOM   2425 N  NZ   . LYS   B 1 35  ? -27.854 65.139 -9.795  1.00 45.56 ? 66  LYS   B NZ   1 
ATOM   2426 N  N    . ARG   B 1 36  ? -27.659 64.652 -14.657 1.00 41.64 ? 67  ARG   B N    1 
ATOM   2427 C  CA   . ARG   B 1 36  ? -26.666 63.599 -14.530 1.00 43.85 ? 67  ARG   B CA   1 
ATOM   2428 C  C    . ARG   B 1 36  ? -26.552 63.183 -13.059 1.00 38.91 ? 67  ARG   B C    1 
ATOM   2429 O  O    . ARG   B 1 36  ? -26.575 64.041 -12.167 1.00 41.34 ? 67  ARG   B O    1 
ATOM   2430 C  CB   . ARG   B 1 36  ? -25.308 64.063 -15.066 1.00 39.36 ? 67  ARG   B CB   1 
ATOM   2431 C  CG   . ARG   B 1 36  ? -24.225 62.990 -15.020 1.00 36.84 ? 67  ARG   B CG   1 
ATOM   2432 C  CD   . ARG   B 1 36  ? -22.975 63.407 -15.766 1.00 40.22 ? 67  ARG   B CD   1 
ATOM   2433 N  NE   . ARG   B 1 36  ? -23.269 63.675 -17.167 1.00 44.42 ? 67  ARG   B NE   1 
ATOM   2434 C  CZ   . ARG   B 1 36  ? -23.381 62.741 -18.100 1.00 45.05 ? 67  ARG   B CZ   1 
ATOM   2435 N  NH1  . ARG   B 1 36  ? -23.191 61.461 -17.825 1.00 40.52 ? 67  ARG   B NH1  1 
ATOM   2436 N  NH2  . ARG   B 1 36  ? -23.704 63.099 -19.339 1.00 45.00 ? 67  ARG   B NH2  1 
ATOM   2437 N  N    . PRO   B 1 37  ? -26.472 61.883 -12.770 1.00 38.58 ? 68  PRO   B N    1 
ATOM   2438 C  CA   . PRO   B 1 37  ? -26.397 61.451 -11.367 1.00 36.82 ? 68  PRO   B CA   1 
ATOM   2439 C  C    . PRO   B 1 37  ? -25.132 61.954 -10.693 1.00 37.71 ? 68  PRO   B C    1 
ATOM   2440 O  O    . PRO   B 1 37  ? -24.098 62.156 -11.328 1.00 38.72 ? 68  PRO   B O    1 
ATOM   2441 C  CB   . PRO   B 1 37  ? -26.409 59.922 -11.457 1.00 34.74 ? 68  PRO   B CB   1 
ATOM   2442 C  CG   . PRO   B 1 37  ? -27.065 59.623 -12.813 1.00 37.79 ? 68  PRO   B CG   1 
ATOM   2443 C  CD   . PRO   B 1 37  ? -26.592 60.744 -13.699 1.00 38.19 ? 68  PRO   B CD   1 
ATOM   2444 N  N    . HIS   B 1 38  ? -25.228 62.151 -9.382  1.00 37.54 ? 69  HIS   B N    1 
ATOM   2445 C  CA   . HIS   B 1 38  ? -24.115 62.651 -8.594  1.00 40.31 ? 69  HIS   B CA   1 
ATOM   2446 C  C    . HIS   B 1 38  ? -24.018 61.850 -7.303  1.00 40.79 ? 69  HIS   B C    1 
ATOM   2447 O  O    . HIS   B 1 38  ? -24.995 61.766 -6.551  1.00 37.92 ? 69  HIS   B O    1 
ATOM   2448 C  CB   . HIS   B 1 38  ? -24.286 64.138 -8.276  1.00 41.71 ? 69  HIS   B CB   1 
ATOM   2449 C  CG   . HIS   B 1 38  ? -23.313 64.645 -7.260  1.00 40.70 ? 69  HIS   B CG   1 
ATOM   2450 N  ND1  . HIS   B 1 38  ? -22.143 65.285 -7.608  1.00 42.80 ? 69  HIS   B ND1  1 
ATOM   2451 C  CD2  . HIS   B 1 38  ? -23.322 64.585 -5.908  1.00 41.92 ? 69  HIS   B CD2  1 
ATOM   2452 C  CE1  . HIS   B 1 38  ? -21.476 65.606 -6.514  1.00 44.97 ? 69  HIS   B CE1  1 
ATOM   2453 N  NE2  . HIS   B 1 38  ? -22.168 65.188 -5.467  1.00 45.98 ? 69  HIS   B NE2  1 
ATOM   2454 N  N    . LEU   B 1 39  ? -22.840 61.288 -7.041  1.00 37.88 ? 70  LEU   B N    1 
ATOM   2455 C  CA   . LEU   B 1 39  ? -22.581 60.522 -5.828  1.00 36.53 ? 70  LEU   B CA   1 
ATOM   2456 C  C    . LEU   B 1 39  ? -21.621 61.283 -4.918  1.00 37.66 ? 70  LEU   B C    1 
ATOM   2457 O  O    . LEU   B 1 39  ? -20.549 61.713 -5.356  1.00 36.40 ? 70  LEU   B O    1 
ATOM   2458 C  CB   . LEU   B 1 39  ? -21.998 59.149 -6.180  1.00 34.50 ? 70  LEU   B CB   1 
ATOM   2459 C  CG   . LEU   B 1 39  ? -21.396 58.317 -5.041  1.00 35.43 ? 70  LEU   B CG   1 
ATOM   2460 C  CD1  . LEU   B 1 39  ? -22.489 57.737 -4.140  1.00 31.67 ? 70  LEU   B CD1  1 
ATOM   2461 C  CD2  . LEU   B 1 39  ? -20.476 57.218 -5.588  1.00 35.52 ? 70  LEU   B CD2  1 
ATOM   2462 N  N    . SER   B 1 40  ? -21.989 61.428 -3.648  1.00 34.72 ? 71  SER   B N    1 
ATOM   2463 C  CA   . SER   B 1 40  ? -21.121 62.036 -2.650  1.00 37.08 ? 71  SER   B CA   1 
ATOM   2464 C  C    . SER   B 1 40  ? -20.640 60.971 -1.676  1.00 35.93 ? 71  SER   B C    1 
ATOM   2465 O  O    . SER   B 1 40  ? -21.452 60.231 -1.109  1.00 34.19 ? 71  SER   B O    1 
ATOM   2466 C  CB   . SER   B 1 40  ? -21.850 63.141 -1.883  1.00 39.98 ? 71  SER   B CB   1 
ATOM   2467 O  OG   . SER   B 1 40  ? -21.953 64.308 -2.665  1.00 37.41 ? 71  SER   B OG   1 
ATOM   2468 N  N    . VAL   B 1 41  ? -19.326 60.889 -1.493  1.00 36.62 ? 72  VAL   B N    1 
ATOM   2469 C  CA   . VAL   B 1 41  ? -18.713 59.980 -0.532  1.00 35.09 ? 72  VAL   B CA   1 
ATOM   2470 C  C    . VAL   B 1 41  ? -18.031 60.819 0.540   1.00 37.75 ? 72  VAL   B C    1 
ATOM   2471 O  O    . VAL   B 1 41  ? -17.244 61.720 0.224   1.00 34.57 ? 72  VAL   B O    1 
ATOM   2472 C  CB   . VAL   B 1 41  ? -17.703 59.031 -1.202  1.00 37.63 ? 72  VAL   B CB   1 
ATOM   2473 C  CG1  . VAL   B 1 41  ? -17.091 58.078 -0.155  1.00 33.74 ? 72  VAL   B CG1  1 
ATOM   2474 C  CG2  . VAL   B 1 41  ? -18.378 58.239 -2.335  1.00 33.25 ? 72  VAL   B CG2  1 
ATOM   2475 N  N    . ILE   B 1 42  ? -18.350 60.545 1.796   1.00 32.76 ? 73  ILE   B N    1 
ATOM   2476 C  CA   . ILE   B 1 42  ? -17.647 61.134 2.930   1.00 37.25 ? 73  ILE   B CA   1 
ATOM   2477 C  C    . ILE   B 1 42  ? -16.647 60.116 3.451   1.00 35.14 ? 73  ILE   B C    1 
ATOM   2478 O  O    . ILE   B 1 42  ? -16.998 58.957 3.703   1.00 36.21 ? 73  ILE   B O    1 
ATOM   2479 C  CB   . ILE   B 1 42  ? -18.616 61.559 4.041   1.00 34.47 ? 73  ILE   B CB   1 
ATOM   2480 C  CG1  . ILE   B 1 42  ? -19.618 62.577 3.498   1.00 36.02 ? 73  ILE   B CG1  1 
ATOM   2481 C  CG2  . ILE   B 1 42  ? -17.815 62.116 5.230   1.00 36.30 ? 73  ILE   B CG2  1 
ATOM   2482 C  CD1  . ILE   B 1 42  ? -20.807 62.823 4.436   1.00 35.44 ? 73  ILE   B CD1  1 
ATOM   2483 N  N    . LEU   B 1 43  ? -15.399 60.545 3.592   1.00 36.36 ? 74  LEU   B N    1 
ATOM   2484 C  CA   . LEU   B 1 43  ? -14.297 59.696 4.009   1.00 35.00 ? 74  LEU   B CA   1 
ATOM   2485 C  C    . LEU   B 1 43  ? -13.638 60.355 5.215   1.00 40.59 ? 74  LEU   B C    1 
ATOM   2486 O  O    . LEU   B 1 43  ? -13.237 61.522 5.144   1.00 39.41 ? 74  LEU   B O    1 
ATOM   2487 C  CB   . LEU   B 1 43  ? -13.310 59.514 2.847   1.00 36.17 ? 74  LEU   B CB   1 
ATOM   2488 C  CG   . LEU   B 1 43  ? -11.962 58.822 3.014   1.00 43.50 ? 74  LEU   B CG   1 
ATOM   2489 C  CD1  . LEU   B 1 43  ? -12.112 57.396 3.519   1.00 39.00 ? 74  LEU   B CD1  1 
ATOM   2490 C  CD2  . LEU   B 1 43  ? -11.236 58.840 1.667   1.00 40.87 ? 74  LEU   B CD2  1 
ATOM   2491 N  N    . VAL   B 1 44  ? -13.552 59.620 6.325   1.00 41.80 ? 75  VAL   B N    1 
ATOM   2492 C  CA   . VAL   B 1 44  ? -13.055 60.134 7.601   1.00 36.89 ? 75  VAL   B CA   1 
ATOM   2493 C  C    . VAL   B 1 44  ? -11.743 59.435 7.921   1.00 37.82 ? 75  VAL   B C    1 
ATOM   2494 O  O    . VAL   B 1 44  ? -11.682 58.199 7.950   1.00 39.54 ? 75  VAL   B O    1 
ATOM   2495 C  CB   . VAL   B 1 44  ? -14.078 59.911 8.729   1.00 38.64 ? 75  VAL   B CB   1 
ATOM   2496 C  CG1  . VAL   B 1 44  ? -13.514 60.371 10.077  1.00 42.34 ? 75  VAL   B CG1  1 
ATOM   2497 C  CG2  . VAL   B 1 44  ? -15.381 60.634 8.418   1.00 34.72 ? 75  VAL   B CG2  1 
ATOM   2498 N  N    . GLY   B 1 45  ? -10.695 60.217 8.169   1.00 39.94 ? 76  GLY   B N    1 
ATOM   2499 C  CA   . GLY   B 1 45  ? -9.456  59.635 8.644   1.00 36.72 ? 76  GLY   B CA   1 
ATOM   2500 C  C    . GLY   B 1 45  ? -8.592  59.087 7.522   1.00 41.07 ? 76  GLY   B C    1 
ATOM   2501 O  O    . GLY   B 1 45  ? -8.782  59.390 6.338   1.00 40.27 ? 76  GLY   B O    1 
ATOM   2502 N  N    . GLU   B 1 46  ? -7.632  58.240 7.908   1.00 39.86 ? 77  GLU   B N    1 
ATOM   2503 C  CA   . GLU   B 1 46  ? -6.533  57.877 7.016   1.00 45.23 ? 77  GLU   B CA   1 
ATOM   2504 C  C    . GLU   B 1 46  ? -6.370  56.366 6.868   1.00 45.66 ? 77  GLU   B C    1 
ATOM   2505 O  O    . GLU   B 1 46  ? -5.268  55.884 6.598   1.00 51.56 ? 77  GLU   B O    1 
ATOM   2506 C  CB   . GLU   B 1 46  ? -5.220  58.499 7.495   1.00 45.46 ? 77  GLU   B CB   1 
ATOM   2507 C  CG   . GLU   B 1 46  ? -5.229  60.014 7.552   1.00 44.39 ? 77  GLU   B CG   1 
ATOM   2508 C  CD   . GLU   B 1 46  ? -3.902  60.586 8.026   1.00 49.08 ? 77  GLU   B CD   1 
ATOM   2509 O  OE1  . GLU   B 1 46  ? -2.935  59.813 8.169   1.00 49.90 ? 77  GLU   B OE1  1 
ATOM   2510 O  OE2  . GLU   B 1 46  ? -3.822  61.812 8.249   1.00 50.62 ? 77  GLU   B OE2  1 
ATOM   2511 N  N    . ASN   B 1 47  ? -7.443  55.608 7.023   1.00 43.71 ? 78  ASN   B N    1 
ATOM   2512 C  CA   . ASN   B 1 47  ? -7.406  54.177 6.756   1.00 41.22 ? 78  ASN   B CA   1 
ATOM   2513 C  C    . ASN   B 1 47  ? -6.966  53.945 5.314   1.00 46.74 ? 78  ASN   B C    1 
ATOM   2514 O  O    . ASN   B 1 47  ? -7.693  54.303 4.380   1.00 46.34 ? 78  ASN   B O    1 
ATOM   2515 C  CB   . ASN   B 1 47  ? -8.782  53.572 7.022   1.00 46.47 ? 78  ASN   B CB   1 
ATOM   2516 C  CG   . ASN   B 1 47  ? -8.768  52.052 7.042   1.00 47.82 ? 78  ASN   B CG   1 
ATOM   2517 O  OD1  . ASN   B 1 47  ? -8.289  51.398 6.107   1.00 41.73 ? 78  ASN   B OD1  1 
ATOM   2518 N  ND2  . ASN   B 1 47  ? -9.306  51.480 8.119   1.00 44.15 ? 78  ASN   B ND2  1 
ATOM   2519 N  N    . PRO   B 1 48  ? -5.774  53.385 5.087   1.00 47.44 ? 79  PRO   B N    1 
ATOM   2520 C  CA   . PRO   B 1 48  ? -5.288  53.255 3.703   1.00 47.65 ? 79  PRO   B CA   1 
ATOM   2521 C  C    . PRO   B 1 48  ? -6.174  52.380 2.836   1.00 47.83 ? 79  PRO   B C    1 
ATOM   2522 O  O    . PRO   B 1 48  ? -6.328  52.662 1.641   1.00 43.22 ? 79  PRO   B O    1 
ATOM   2523 C  CB   . PRO   B 1 48  ? -3.880  52.664 3.874   1.00 46.34 ? 79  PRO   B CB   1 
ATOM   2524 C  CG   . PRO   B 1 48  ? -3.866  52.055 5.217   1.00 47.87 ? 79  PRO   B CG   1 
ATOM   2525 C  CD   . PRO   B 1 48  ? -4.832  52.821 6.072   1.00 45.11 ? 79  PRO   B CD   1 
ATOM   2526 N  N    . ALA   B 1 49  ? -6.780  51.336 3.407   1.00 45.81 ? 80  ALA   B N    1 
ATOM   2527 C  CA   . ALA   B 1 49  ? -7.722  50.528 2.644   1.00 46.69 ? 80  ALA   B CA   1 
ATOM   2528 C  C    . ALA   B 1 49  ? -8.954  51.343 2.253   1.00 44.99 ? 80  ALA   B C    1 
ATOM   2529 O  O    . ALA   B 1 49  ? -9.421  51.270 1.108   1.00 42.80 ? 80  ALA   B O    1 
ATOM   2530 C  CB   . ALA   B 1 49  ? -8.107  49.287 3.453   1.00 44.68 ? 80  ALA   B CB   1 
ATOM   2531 N  N    . SER   B 1 50  ? -9.477  52.144 3.186   1.00 41.29 ? 81  SER   B N    1 
ATOM   2532 C  CA   . SER   B 1 50  ? -10.655 52.964 2.909   1.00 40.54 ? 81  SER   B CA   1 
ATOM   2533 C  C    . SER   B 1 50  ? -10.408 53.924 1.749   1.00 41.38 ? 81  SER   B C    1 
ATOM   2534 O  O    . SER   B 1 50  ? -11.242 54.050 0.843   1.00 39.45 ? 81  SER   B O    1 
ATOM   2535 C  CB   . SER   B 1 50  ? -11.047 53.746 4.165   1.00 39.60 ? 81  SER   B CB   1 
ATOM   2536 O  OG   . SER   B 1 50  ? -11.375 52.863 5.231   1.00 42.71 ? 81  SER   B OG   1 
ATOM   2537 N  N    . HIS   B 1 51  ? -9.270  54.622 1.766   1.00 42.27 ? 82  HIS   B N    1 
ATOM   2538 C  CA   . HIS   B 1 51  ? -8.969  55.556 0.684   1.00 43.93 ? 82  HIS   B CA   1 
ATOM   2539 C  C    . HIS   B 1 51  ? -8.862  54.828 -0.647  1.00 42.61 ? 82  HIS   B C    1 
ATOM   2540 O  O    . HIS   B 1 51  ? -9.377  55.293 -1.673  1.00 42.41 ? 82  HIS   B O    1 
ATOM   2541 C  CB   . HIS   B 1 51  ? -7.674  56.304 0.989   1.00 44.75 ? 82  HIS   B CB   1 
ATOM   2542 C  CG   . HIS   B 1 51  ? -7.828  57.367 2.027   1.00 45.58 ? 82  HIS   B CG   1 
ATOM   2543 N  ND1  . HIS   B 1 51  ? -7.841  58.711 1.717   1.00 49.21 ? 82  HIS   B ND1  1 
ATOM   2544 C  CD2  . HIS   B 1 51  ? -7.999  57.287 3.368   1.00 43.37 ? 82  HIS   B CD2  1 
ATOM   2545 C  CE1  . HIS   B 1 51  ? -7.996  59.414 2.828   1.00 46.72 ? 82  HIS   B CE1  1 
ATOM   2546 N  NE2  . HIS   B 1 51  ? -8.093  58.573 3.842   1.00 41.42 ? 82  HIS   B NE2  1 
ATOM   2547 N  N    . SER   B 1 52  ? -8.199  53.678 -0.643  1.00 40.42 ? 83  SER   B N    1 
ATOM   2548 C  CA   . SER   B 1 52  ? -8.088  52.888 -1.856  1.00 45.46 ? 83  SER   B CA   1 
ATOM   2549 C  C    . SER   B 1 52  ? -9.474  52.523 -2.383  1.00 44.27 ? 83  SER   B C    1 
ATOM   2550 O  O    . SER   B 1 52  ? -9.788  52.762 -3.554  1.00 40.56 ? 83  SER   B O    1 
ATOM   2551 C  CB   . SER   B 1 52  ? -7.242  51.644 -1.557  1.00 43.17 ? 83  SER   B CB   1 
ATOM   2552 O  OG   . SER   B 1 52  ? -6.862  50.991 -2.748  1.00 57.49 ? 83  SER   B OG   1 
ATOM   2553 N  N    . TYR   B 1 53  ? -10.345 52.010 -1.500  1.00 40.88 ? 84  TYR   B N    1 
ATOM   2554 C  CA   . TYR   B 1 53  ? -11.672 51.566 -1.917  1.00 39.18 ? 84  TYR   B CA   1 
ATOM   2555 C  C    . TYR   B 1 53  ? -12.523 52.732 -2.402  1.00 36.12 ? 84  TYR   B C    1 
ATOM   2556 O  O    . TYR   B 1 53  ? -13.290 52.583 -3.353  1.00 35.47 ? 84  TYR   B O    1 
ATOM   2557 C  CB   . TYR   B 1 53  ? -12.381 50.836 -0.763  1.00 40.40 ? 84  TYR   B CB   1 
ATOM   2558 C  CG   . TYR   B 1 53  ? -11.626 49.636 -0.231  1.00 42.25 ? 84  TYR   B CG   1 
ATOM   2559 C  CD1  . TYR   B 1 53  ? -11.847 49.172 1.060   1.00 42.84 ? 84  TYR   B CD1  1 
ATOM   2560 C  CD2  . TYR   B 1 53  ? -10.692 48.968 -1.020  1.00 42.96 ? 84  TYR   B CD2  1 
ATOM   2561 C  CE1  . TYR   B 1 53  ? -11.153 48.078 1.560   1.00 46.02 ? 84  TYR   B CE1  1 
ATOM   2562 C  CE2  . TYR   B 1 53  ? -9.994  47.874 -0.535  1.00 46.55 ? 84  TYR   B CE2  1 
ATOM   2563 C  CZ   . TYR   B 1 53  ? -10.230 47.433 0.759   1.00 51.12 ? 84  TYR   B CZ   1 
ATOM   2564 O  OH   . TYR   B 1 53  ? -9.539  46.350 1.251   1.00 50.84 ? 84  TYR   B OH   1 
ATOM   2565 N  N    . VAL   B 1 54  ? -12.426 53.887 -1.736  1.00 35.25 ? 85  VAL   B N    1 
ATOM   2566 C  CA   . VAL   B 1 54  ? -13.180 55.071 -2.143  1.00 34.40 ? 85  VAL   B CA   1 
ATOM   2567 C  C    . VAL   B 1 54  ? -12.710 55.574 -3.513  1.00 38.58 ? 85  VAL   B C    1 
ATOM   2568 O  O    . VAL   B 1 54  ? -13.522 55.978 -4.352  1.00 37.00 ? 85  VAL   B O    1 
ATOM   2569 C  CB   . VAL   B 1 54  ? -13.070 56.157 -1.052  1.00 39.43 ? 85  VAL   B CB   1 
ATOM   2570 C  CG1  . VAL   B 1 54  ? -13.556 57.500 -1.565  1.00 40.71 ? 85  VAL   B CG1  1 
ATOM   2571 C  CG2  . VAL   B 1 54  ? -13.885 55.756 0.194   1.00 34.82 ? 85  VAL   B CG2  1 
ATOM   2572 N  N    . LEU   B 1 55  ? -11.400 55.549 -3.767  1.00 37.14 ? 86  LEU   B N    1 
ATOM   2573 C  CA   . LEU   B 1 55  ? -10.906 55.961 -5.083  1.00 36.92 ? 86  LEU   B CA   1 
ATOM   2574 C  C    . LEU   B 1 55  ? -11.420 55.026 -6.178  1.00 36.94 ? 86  LEU   B C    1 
ATOM   2575 O  O    . LEU   B 1 55  ? -11.809 55.477 -7.268  1.00 38.73 ? 86  LEU   B O    1 
ATOM   2576 C  CB   . LEU   B 1 55  ? -9.370  56.011 -5.074  1.00 37.18 ? 86  LEU   B CB   1 
ATOM   2577 C  CG   . LEU   B 1 55  ? -8.689  56.272 -6.424  1.00 46.38 ? 86  LEU   B CG   1 
ATOM   2578 C  CD1  . LEU   B 1 55  ? -9.142  57.613 -6.993  1.00 46.52 ? 86  LEU   B CD1  1 
ATOM   2579 C  CD2  . LEU   B 1 55  ? -7.161  56.198 -6.308  1.00 45.37 ? 86  LEU   B CD2  1 
ATOM   2580 N  N    . ASN   B 1 56  ? -11.433 53.719 -5.902  1.00 34.08 ? 87  ASN   B N    1 
ATOM   2581 C  CA   . ASN   B 1 56  ? -12.012 52.765 -6.835  1.00 39.32 ? 87  ASN   B CA   1 
ATOM   2582 C  C    . ASN   B 1 56  ? -13.467 53.106 -7.129  1.00 38.44 ? 87  ASN   B C    1 
ATOM   2583 O  O    . ASN   B 1 56  ? -13.909 53.014 -8.278  1.00 37.71 ? 87  ASN   B O    1 
ATOM   2584 C  CB   . ASN   B 1 56  ? -11.890 51.345 -6.281  1.00 38.39 ? 87  ASN   B CB   1 
ATOM   2585 C  CG   . ASN   B 1 56  ? -10.457 50.804 -6.336  1.00 44.56 ? 87  ASN   B CG   1 
ATOM   2586 O  OD1  . ASN   B 1 56  ? -9.572  51.405 -6.952  1.00 43.65 ? 87  ASN   B OD1  1 
ATOM   2587 N  ND2  . ASN   B 1 56  ? -10.232 49.651 -5.705  1.00 44.66 ? 87  ASN   B ND2  1 
ATOM   2588 N  N    . LYS   B 1 57  ? -14.222 53.519 -6.102  1.00 35.52 ? 88  LYS   B N    1 
ATOM   2589 C  CA   . LYS   B 1 57  ? -15.623 53.890 -6.292  1.00 35.59 ? 88  LYS   B CA   1 
ATOM   2590 C  C    . LYS   B 1 57  ? -15.758 55.124 -7.189  1.00 34.81 ? 88  LYS   B C    1 
ATOM   2591 O  O    . LYS   B 1 57  ? -16.561 55.138 -8.130  1.00 37.20 ? 88  LYS   B O    1 
ATOM   2592 C  CB   . LYS   B 1 57  ? -16.286 54.121 -4.920  1.00 34.22 ? 88  LYS   B CB   1 
ATOM   2593 C  CG   . LYS   B 1 57  ? -16.408 52.827 -4.097  1.00 29.96 ? 88  LYS   B CG   1 
ATOM   2594 C  CD   . LYS   B 1 57  ? -16.849 53.018 -2.643  1.00 31.59 ? 88  LYS   B CD   1 
ATOM   2595 C  CE   . LYS   B 1 57  ? -16.744 51.684 -1.913  1.00 33.26 ? 88  LYS   B CE   1 
ATOM   2596 N  NZ   . LYS   B 1 57  ? -17.411 51.707 -0.572  1.00 34.79 ? 88  LYS   B NZ   1 
ATOM   2597 N  N    . THR   B 1 58  ? -14.969 56.169 -6.926  1.00 32.79 ? 89  THR   B N    1 
ATOM   2598 C  CA   . THR   B 1 58  ? -15.135 57.400 -7.695  1.00 35.57 ? 89  THR   B CA   1 
ATOM   2599 C  C    . THR   B 1 58  ? -14.569 57.262 -9.105  1.00 33.08 ? 89  THR   B C    1 
ATOM   2600 O  O    . THR   B 1 58  ? -15.110 57.857 -10.042 1.00 34.96 ? 89  THR   B O    1 
ATOM   2601 C  CB   . THR   B 1 58  ? -14.500 58.574 -6.952  1.00 33.73 ? 89  THR   B CB   1 
ATOM   2602 O  OG1  . THR   B 1 58  ? -13.112 58.307 -6.733  1.00 36.77 ? 89  THR   B OG1  1 
ATOM   2603 C  CG2  . THR   B 1 58  ? -15.178 58.741 -5.598  1.00 37.22 ? 89  THR   B CG2  1 
ATOM   2604 N  N    . ARG   B 1 59  ? -13.518 56.452 -9.284  1.00 34.24 ? 90  ARG   B N    1 
ATOM   2605 C  CA   . ARG   B 1 59  ? -13.065 56.122 -10.636 1.00 36.38 ? 90  ARG   B CA   1 
ATOM   2606 C  C    . ARG   B 1 59  ? -14.158 55.411 -11.421 1.00 37.80 ? 90  ARG   B C    1 
ATOM   2607 O  O    . ARG   B 1 59  ? -14.369 55.695 -12.605 1.00 39.83 ? 90  ARG   B O    1 
ATOM   2608 C  CB   . ARG   B 1 59  ? -11.831 55.224 -10.594 1.00 38.61 ? 90  ARG   B CB   1 
ATOM   2609 C  CG   . ARG   B 1 59  ? -10.536 55.877 -10.207 1.00 41.13 ? 90  ARG   B CG   1 
ATOM   2610 C  CD   . ARG   B 1 59  ? -9.489  54.799 -10.058 1.00 38.91 ? 90  ARG   B CD   1 
ATOM   2611 N  NE   . ARG   B 1 59  ? -8.152  55.352 -9.908  1.00 44.98 ? 90  ARG   B NE   1 
ATOM   2612 C  CZ   . ARG   B 1 59  ? -7.088  54.631 -9.585  1.00 51.65 ? 90  ARG   B CZ   1 
ATOM   2613 N  NH1  . ARG   B 1 59  ? -7.188  53.340 -9.302  1.00 54.33 ? 90  ARG   B NH1  1 
ATOM   2614 N  NH2  . ARG   B 1 59  ? -5.892  55.218 -9.546  1.00 47.53 ? 90  ARG   B NH2  1 
ATOM   2615 N  N    . ALA   B 1 60  ? -14.840 54.452 -10.789 1.00 37.25 ? 91  ALA   B N    1 
ATOM   2616 C  CA   . ALA   B 1 60  ? -15.904 53.742 -11.493 1.00 38.07 ? 91  ALA   B CA   1 
ATOM   2617 C  C    . ALA   B 1 60  ? -17.062 54.676 -11.806 1.00 36.96 ? 91  ALA   B C    1 
ATOM   2618 O  O    . ALA   B 1 60  ? -17.665 54.582 -12.880 1.00 37.60 ? 91  ALA   B O    1 
ATOM   2619 C  CB   . ALA   B 1 60  ? -16.375 52.543 -10.669 1.00 36.77 ? 91  ALA   B CB   1 
ATOM   2620 N  N    . ALA   B 1 61  ? -17.374 55.597 -10.883 1.00 31.33 ? 92  ALA   B N    1 
ATOM   2621 C  CA   . ALA   B 1 61  ? -18.422 56.585 -11.130 1.00 34.21 ? 92  ALA   B CA   1 
ATOM   2622 C  C    . ALA   B 1 61  ? -18.126 57.412 -12.385 1.00 37.45 ? 92  ALA   B C    1 
ATOM   2623 O  O    . ALA   B 1 61  ? -18.986 57.560 -13.261 1.00 35.75 ? 92  ALA   B O    1 
ATOM   2624 C  CB   . ALA   B 1 61  ? -18.578 57.493 -9.911  1.00 34.41 ? 92  ALA   B CB   1 
ATOM   2625 N  N    . ALA   B 1 62  ? -16.908 57.951 -12.493 1.00 35.57 ? 93  ALA   B N    1 
ATOM   2626 C  CA   . ALA   B 1 62  ? -16.551 58.753 -13.663 1.00 38.25 ? 93  ALA   B CA   1 
ATOM   2627 C  C    . ALA   B 1 62  ? -16.744 57.963 -14.951 1.00 39.98 ? 93  ALA   B C    1 
ATOM   2628 O  O    . ALA   B 1 62  ? -17.316 58.468 -15.925 1.00 38.58 ? 93  ALA   B O    1 
ATOM   2629 C  CB   . ALA   B 1 62  ? -15.100 59.234 -13.561 1.00 39.23 ? 93  ALA   B CB   1 
ATOM   2630 N  N    . VAL   B 1 63  ? -16.303 56.708 -14.956 1.00 37.77 ? 94  VAL   B N    1 
ATOM   2631 C  CA   . VAL   B 1 63  ? -16.346 55.892 -16.163 1.00 45.91 ? 94  VAL   B CA   1 
ATOM   2632 C  C    . VAL   B 1 63  ? -17.773 55.623 -16.622 1.00 42.95 ? 94  VAL   B C    1 
ATOM   2633 O  O    . VAL   B 1 63  ? -18.016 55.477 -17.820 1.00 40.07 ? 94  VAL   B O    1 
ATOM   2634 C  CB   . VAL   B 1 63  ? -15.550 54.602 -15.914 1.00 47.22 ? 94  VAL   B CB   1 
ATOM   2635 C  CG1  . VAL   B 1 63  ? -16.066 53.461 -16.771 1.00 56.11 ? 94  VAL   B CG1  1 
ATOM   2636 C  CG2  . VAL   B 1 63  ? -14.123 54.881 -16.263 1.00 49.25 ? 94  VAL   B CG2  1 
ATOM   2637 N  N    . VAL   B 1 64  ? -18.740 55.557 -15.705 1.00 37.73 ? 95  VAL   B N    1 
ATOM   2638 C  CA   . VAL   B 1 64  ? -20.112 55.255 -16.100 1.00 38.74 ? 95  VAL   B CA   1 
ATOM   2639 C  C    . VAL   B 1 64  ? -20.961 56.518 -16.253 1.00 37.71 ? 95  VAL   B C    1 
ATOM   2640 O  O    . VAL   B 1 64  ? -22.182 56.424 -16.402 1.00 37.69 ? 95  VAL   B O    1 
ATOM   2641 C  CB   . VAL   B 1 64  ? -20.760 54.253 -15.129 1.00 42.41 ? 95  VAL   B CB   1 
ATOM   2642 C  CG1  . VAL   B 1 64  ? -19.934 52.968 -15.083 1.00 38.96 ? 95  VAL   B CG1  1 
ATOM   2643 C  CG2  . VAL   B 1 64  ? -20.921 54.851 -13.721 1.00 35.65 ? 95  VAL   B CG2  1 
ATOM   2644 N  N    . GLY   B 1 65  ? -20.346 57.698 -16.227 1.00 35.18 ? 96  GLY   B N    1 
ATOM   2645 C  CA   . GLY   B 1 65  ? -21.101 58.924 -16.401 1.00 34.63 ? 96  GLY   B CA   1 
ATOM   2646 C  C    . GLY   B 1 65  ? -21.774 59.468 -15.161 1.00 38.49 ? 96  GLY   B C    1 
ATOM   2647 O  O    . GLY   B 1 65  ? -22.701 60.278 -15.278 1.00 34.48 ? 96  GLY   B O    1 
ATOM   2648 N  N    . ILE   B 1 66  ? -21.344 59.052 -13.973 1.00 35.72 ? 97  ILE   B N    1 
ATOM   2649 C  CA   . ILE   B 1 66  ? -21.890 59.556 -12.717 1.00 36.57 ? 97  ILE   B CA   1 
ATOM   2650 C  C    . ILE   B 1 66  ? -20.891 60.546 -12.125 1.00 34.29 ? 97  ILE   B C    1 
ATOM   2651 O  O    . ILE   B 1 66  ? -19.722 60.207 -11.910 1.00 37.05 ? 97  ILE   B O    1 
ATOM   2652 C  CB   . ILE   B 1 66  ? -22.191 58.402 -11.744 1.00 35.01 ? 97  ILE   B CB   1 
ATOM   2653 C  CG1  . ILE   B 1 66  ? -23.284 57.494 -12.330 1.00 34.38 ? 97  ILE   B CG1  1 
ATOM   2654 C  CG2  . ILE   B 1 66  ? -22.570 58.948 -10.343 1.00 32.33 ? 97  ILE   B CG2  1 
ATOM   2655 C  CD1  . ILE   B 1 66  ? -23.459 56.160 -11.599 1.00 33.47 ? 97  ILE   B CD1  1 
ATOM   2656 N  N    . ASN   B 1 67  ? -21.332 61.776 -11.885 1.00 33.65 ? 98  ASN   B N    1 
ATOM   2657 C  CA   . ASN   B 1 67  ? -20.487 62.752 -11.217 1.00 35.55 ? 98  ASN   B CA   1 
ATOM   2658 C  C    . ASN   B 1 67  ? -20.261 62.348 -9.760  1.00 38.17 ? 98  ASN   B C    1 
ATOM   2659 O  O    . ASN   B 1 67  ? -21.078 61.657 -9.149  1.00 36.49 ? 98  ASN   B O    1 
ATOM   2660 C  CB   . ASN   B 1 67  ? -21.126 64.137 -11.262 1.00 40.12 ? 98  ASN   B CB   1 
ATOM   2661 C  CG   . ASN   B 1 67  ? -21.137 64.720 -12.645 1.00 47.97 ? 98  ASN   B CG   1 
ATOM   2662 O  OD1  . ASN   B 1 67  ? -20.295 64.369 -13.476 1.00 46.37 ? 98  ASN   B OD1  1 
ATOM   2663 N  ND2  . ASN   B 1 67  ? -22.092 65.615 -12.911 1.00 44.35 ? 98  ASN   B ND2  1 
ATOM   2664 N  N    . SER   B 1 68  ? -19.138 62.780 -9.197  1.00 37.81 ? 99  SER   B N    1 
ATOM   2665 C  CA   . SER   B 1 68  ? -18.901 62.464 -7.793  1.00 40.81 ? 99  SER   B CA   1 
ATOM   2666 C  C    . SER   B 1 68  ? -17.994 63.496 -7.147  1.00 39.71 ? 99  SER   B C    1 
ATOM   2667 O  O    . SER   B 1 68  ? -17.268 64.234 -7.823  1.00 37.12 ? 99  SER   B O    1 
ATOM   2668 C  CB   . SER   B 1 68  ? -18.277 61.080 -7.628  1.00 36.46 ? 99  SER   B CB   1 
ATOM   2669 O  OG   . SER   B 1 68  ? -16.969 61.070 -8.171  1.00 42.20 ? 99  SER   B OG   1 
ATOM   2670 N  N    . GLU   B 1 69  ? -18.037 63.520 -5.812  1.00 40.55 ? 100 GLU   B N    1 
ATOM   2671 C  CA   . GLU   B 1 69  ? -17.054 64.211 -4.991  1.00 42.41 ? 100 GLU   B CA   1 
ATOM   2672 C  C    . GLU   B 1 69  ? -16.752 63.348 -3.773  1.00 40.40 ? 100 GLU   B C    1 
ATOM   2673 O  O    . GLU   B 1 69  ? -17.657 62.726 -3.205  1.00 43.30 ? 100 GLU   B O    1 
ATOM   2674 C  CB   . GLU   B 1 69  ? -17.551 65.596 -4.542  1.00 44.26 ? 100 GLU   B CB   1 
ATOM   2675 C  CG   . GLU   B 1 69  ? -18.734 65.529 -3.597  1.00 44.77 ? 100 GLU   B CG   1 
ATOM   2676 C  CD   . GLU   B 1 69  ? -19.422 66.867 -3.368  1.00 48.51 ? 100 GLU   B CD   1 
ATOM   2677 O  OE1  . GLU   B 1 69  ? -18.774 67.912 -3.600  1.00 43.12 ? 100 GLU   B OE1  1 
ATOM   2678 O  OE2  . GLU   B 1 69  ? -20.615 66.859 -2.954  1.00 47.84 ? 100 GLU   B OE2  1 
ATOM   2679 N  N    . THR   B 1 70  ? -15.482 63.290 -3.388  1.00 35.13 ? 101 THR   B N    1 
ATOM   2680 C  CA   . THR   B 1 70  ? -15.098 62.703 -2.110  1.00 38.75 ? 101 THR   B CA   1 
ATOM   2681 C  C    . THR   B 1 70  ? -14.818 63.838 -1.126  1.00 41.99 ? 101 THR   B C    1 
ATOM   2682 O  O    . THR   B 1 70  ? -13.989 64.714 -1.396  1.00 39.59 ? 101 THR   B O    1 
ATOM   2683 C  CB   . THR   B 1 70  ? -13.876 61.796 -2.256  1.00 41.89 ? 101 THR   B CB   1 
ATOM   2684 O  OG1  . THR   B 1 70  ? -14.158 60.773 -3.215  1.00 44.52 ? 101 THR   B OG1  1 
ATOM   2685 C  CG2  . THR   B 1 70  ? -13.521 61.141 -0.928  1.00 40.75 ? 101 THR   B CG2  1 
ATOM   2686 N  N    . ILE   B 1 71  ? -15.515 63.830 0.003   1.00 39.71 ? 102 ILE   B N    1 
ATOM   2687 C  CA   . ILE   B 1 71  ? -15.321 64.830 1.039   1.00 39.05 ? 102 ILE   B CA   1 
ATOM   2688 C  C    . ILE   B 1 71  ? -14.552 64.155 2.163   1.00 41.71 ? 102 ILE   B C    1 
ATOM   2689 O  O    . ILE   B 1 71  ? -15.090 63.289 2.862   1.00 37.32 ? 102 ILE   B O    1 
ATOM   2690 C  CB   . ILE   B 1 71  ? -16.655 65.410 1.512   1.00 38.38 ? 102 ILE   B CB   1 
ATOM   2691 C  CG1  . ILE   B 1 71  ? -17.418 65.973 0.303   1.00 42.09 ? 102 ILE   B CG1  1 
ATOM   2692 C  CG2  . ILE   B 1 71  ? -16.413 66.481 2.549   1.00 41.84 ? 102 ILE   B CG2  1 
ATOM   2693 C  CD1  . ILE   B 1 71  ? -18.883 66.227 0.568   1.00 44.05 ? 102 ILE   B CD1  1 
ATOM   2694 N  N    . MET   B 1 72  ? -13.273 64.502 2.293   1.00 37.84 ? 103 MET   B N    1 
ATOM   2695 C  CA   . MET   B 1 72  ? -12.399 63.903 3.291   1.00 42.67 ? 103 MET   B CA   1 
ATOM   2696 C  C    . MET   B 1 72  ? -12.342 64.807 4.514   1.00 41.00 ? 103 MET   B C    1 
ATOM   2697 O  O    . MET   B 1 72  ? -12.178 66.026 4.389   1.00 38.58 ? 103 MET   B O    1 
ATOM   2698 C  CB   . MET   B 1 72  ? -10.993 63.666 2.735   1.00 40.57 ? 103 MET   B CB   1 
ATOM   2699 C  CG   . MET   B 1 72  ? -10.991 63.215 1.280   1.00 50.54 ? 103 MET   B CG   1 
ATOM   2700 S  SD   . MET   B 1 72  ? -9.377  62.772 0.599   1.00 61.90 ? 103 MET   B SD   1 
ATOM   2701 C  CE   . MET   B 1 72  ? -9.748  62.786 -1.165  1.00 50.89 ? 103 MET   B CE   1 
ATOM   2702 N  N    . LYS   B 1 73  ? -12.493 64.203 5.687   1.00 40.21 ? 104 LYS   B N    1 
ATOM   2703 C  CA   . LYS   B 1 73  ? -12.473 64.874 6.970   1.00 39.67 ? 104 LYS   B CA   1 
ATOM   2704 C  C    . LYS   B 1 73  ? -11.449 64.191 7.859   1.00 40.80 ? 104 LYS   B C    1 
ATOM   2705 O  O    . LYS   B 1 73  ? -11.225 62.980 7.732   1.00 37.13 ? 104 LYS   B O    1 
ATOM   2706 C  CB   . LYS   B 1 73  ? -13.845 64.817 7.657   1.00 41.75 ? 104 LYS   B CB   1 
ATOM   2707 C  CG   . LYS   B 1 73  ? -14.998 65.328 6.825   1.00 40.53 ? 104 LYS   B CG   1 
ATOM   2708 C  CD   . LYS   B 1 73  ? -14.942 66.832 6.641   1.00 40.17 ? 104 LYS   B CD   1 
ATOM   2709 C  CE   . LYS   B 1 73  ? -15.078 67.576 7.957   1.00 46.18 ? 104 LYS   B CE   1 
ATOM   2710 N  NZ   . LYS   B 1 73  ? -15.285 69.038 7.724   1.00 47.30 ? 104 LYS   B NZ   1 
ATOM   2711 N  N    . PRO   B 1 74  ? -10.824 64.931 8.774   1.00 40.10 ? 105 PRO   B N    1 
ATOM   2712 C  CA   . PRO   B 1 74  ? -9.867  64.300 9.684   1.00 40.60 ? 105 PRO   B CA   1 
ATOM   2713 C  C    . PRO   B 1 74  ? -10.587 63.370 10.648  1.00 41.13 ? 105 PRO   B C    1 
ATOM   2714 O  O    . PRO   B 1 74  ? -11.778 63.540 10.939  1.00 36.23 ? 105 PRO   B O    1 
ATOM   2715 C  CB   . PRO   B 1 74  ? -9.235  65.490 10.416  1.00 41.80 ? 105 PRO   B CB   1 
ATOM   2716 C  CG   . PRO   B 1 74  ? -10.330 66.488 10.473  1.00 42.89 ? 105 PRO   B CG   1 
ATOM   2717 C  CD   . PRO   B 1 74  ? -11.062 66.345 9.134   1.00 40.23 ? 105 PRO   B CD   1 
ATOM   2718 N  N    . ALA   B 1 75  ? -9.838  62.368 11.134  1.00 38.93 ? 106 ALA   B N    1 
ATOM   2719 C  CA   . ALA   B 1 75  ? -10.369 61.426 12.116  1.00 40.90 ? 106 ALA   B CA   1 
ATOM   2720 C  C    . ALA   B 1 75  ? -10.757 62.105 13.420  1.00 46.55 ? 106 ALA   B C    1 
ATOM   2721 O  O    . ALA   B 1 75  ? -11.538 61.535 14.188  1.00 45.30 ? 106 ALA   B O    1 
ATOM   2722 C  CB   . ALA   B 1 75  ? -9.352  60.322 12.410  1.00 38.61 ? 106 ALA   B CB   1 
ATOM   2723 N  N    . SER   B 1 76  ? -10.225 63.301 13.688  1.00 45.18 ? 107 SER   B N    1 
ATOM   2724 C  CA   . SER   B 1 76  ? -10.561 64.081 14.875  1.00 47.15 ? 107 SER   B CA   1 
ATOM   2725 C  C    . SER   B 1 76  ? -11.922 64.755 14.779  1.00 46.78 ? 107 SER   B C    1 
ATOM   2726 O  O    . SER   B 1 76  ? -12.340 65.420 15.733  1.00 47.16 ? 107 SER   B O    1 
ATOM   2727 C  CB   . SER   B 1 76  ? -9.484  65.143 15.122  1.00 46.25 ? 107 SER   B CB   1 
ATOM   2728 O  OG   . SER   B 1 76  ? -9.239  65.900 13.939  1.00 46.18 ? 107 SER   B OG   1 
ATOM   2729 N  N    . ILE   B 1 77  ? -12.608 64.631 13.644  1.00 43.20 ? 108 ILE   B N    1 
ATOM   2730 C  CA   . ILE   B 1 77  ? -13.939 65.208 13.513  1.00 43.17 ? 108 ILE   B CA   1 
ATOM   2731 C  C    . ILE   B 1 77  ? -14.832 64.652 14.616  1.00 47.76 ? 108 ILE   B C    1 
ATOM   2732 O  O    . ILE   B 1 77  ? -14.682 63.497 15.038  1.00 44.60 ? 108 ILE   B O    1 
ATOM   2733 C  CB   . ILE   B 1 77  ? -14.505 64.904 12.113  1.00 45.07 ? 108 ILE   B CB   1 
ATOM   2734 C  CG1  . ILE   B 1 77  ? -15.878 65.534 11.927  1.00 46.05 ? 108 ILE   B CG1  1 
ATOM   2735 C  CG2  . ILE   B 1 77  ? -14.627 63.400 11.886  1.00 40.14 ? 108 ILE   B CG2  1 
ATOM   2736 C  CD1  . ILE   B 1 77  ? -16.370 65.431 10.487  1.00 50.91 ? 108 ILE   B CD1  1 
ATOM   2737 N  N    . SER   B 1 78  ? -15.744 65.483 15.113  1.00 48.73 ? 109 SER   B N    1 
ATOM   2738 C  CA   . SER   B 1 78  ? -16.714 65.032 16.099  1.00 49.97 ? 109 SER   B CA   1 
ATOM   2739 C  C    . SER   B 1 78  ? -17.970 64.524 15.404  1.00 49.22 ? 109 SER   B C    1 
ATOM   2740 O  O    . SER   B 1 78  ? -18.226 64.812 14.233  1.00 46.23 ? 109 SER   B O    1 
ATOM   2741 C  CB   . SER   B 1 78  ? -17.089 66.155 17.063  1.00 49.36 ? 109 SER   B CB   1 
ATOM   2742 O  OG   . SER   B 1 78  ? -18.158 66.915 16.526  1.00 50.44 ? 109 SER   B OG   1 
ATOM   2743 N  N    . GLU   B 1 79  ? -18.773 63.781 16.161  1.00 43.70 ? 110 GLU   B N    1 
ATOM   2744 C  CA   . GLU   B 1 79  ? -19.994 63.205 15.614  1.00 48.01 ? 110 GLU   B CA   1 
ATOM   2745 C  C    . GLU   B 1 79  ? -20.972 64.289 15.180  1.00 49.11 ? 110 GLU   B C    1 
ATOM   2746 O  O    . GLU   B 1 79  ? -21.637 64.154 14.144  1.00 42.71 ? 110 GLU   B O    1 
ATOM   2747 C  CB   . GLU   B 1 79  ? -20.633 62.266 16.641  1.00 47.88 ? 110 GLU   B CB   1 
ATOM   2748 C  CG   . GLU   B 1 79  ? -21.955 61.673 16.206  1.00 50.12 ? 110 GLU   B CG   1 
ATOM   2749 C  CD   . GLU   B 1 79  ? -22.445 60.588 17.144  1.00 55.36 ? 110 GLU   B CD   1 
ATOM   2750 O  OE1  . GLU   B 1 79  ? -21.691 59.618 17.389  1.00 56.02 ? 110 GLU   B OE1  1 
ATOM   2751 O  OE2  . GLU   B 1 79  ? -23.587 60.710 17.634  1.00 55.25 ? 110 GLU   B OE2  1 
ATOM   2752 N  N    . GLU   B 1 80  ? -21.077 65.370 15.957  1.00 46.78 ? 111 GLU   B N    1 
ATOM   2753 C  CA   . GLU   B 1 80  ? -21.960 66.468 15.564  1.00 48.15 ? 111 GLU   B CA   1 
ATOM   2754 C  C    . GLU   B 1 80  ? -21.511 67.096 14.247  1.00 46.34 ? 111 GLU   B C    1 
ATOM   2755 O  O    . GLU   B 1 80  ? -22.344 67.531 13.442  1.00 44.77 ? 111 GLU   B O    1 
ATOM   2756 C  CB   . GLU   B 1 80  ? -22.021 67.536 16.661  1.00 53.46 ? 111 GLU   B CB   1 
ATOM   2757 C  CG   . GLU   B 1 80  ? -22.579 67.053 18.002  1.00 57.34 ? 111 GLU   B CG   1 
ATOM   2758 C  CD   . GLU   B 1 80  ? -21.509 66.480 18.934  1.00 64.76 ? 111 GLU   B CD   1 
ATOM   2759 O  OE1  . GLU   B 1 80  ? -20.886 65.438 18.607  1.00 58.82 ? 111 GLU   B OE1  1 
ATOM   2760 O  OE2  . GLU   B 1 80  ? -21.285 67.087 20.006  1.00 73.55 ? 111 GLU   B OE2  1 
ATOM   2761 N  N    . GLU   B 1 81  ? -20.206 67.157 14.026  1.00 46.61 ? 112 GLU   B N    1 
ATOM   2762 C  CA   . GLU   B 1 81  ? -19.683 67.806 12.799  1.00 49.16 ? 112 GLU   B CA   1 
ATOM   2763 C  C    . GLU   B 1 81  ? -20.022 66.923 11.596  1.00 45.73 ? 112 GLU   B C    1 
ATOM   2764 O  O    . GLU   B 1 81  ? -20.446 67.466 10.573  1.00 44.12 ? 112 GLU   B O    1 
ATOM   2765 C  CB   . GLU   B 1 81  ? -18.188 68.056 12.979  1.00 50.71 ? 112 GLU   B CB   1 
ATOM   2766 C  CG   . GLU   B 1 81  ? -17.828 68.471 14.392  1.00 57.75 ? 112 GLU   B CG   1 
ATOM   2767 C  CD   . GLU   B 1 81  ? -16.644 69.412 14.525  1.00 66.57 ? 112 GLU   B CD   1 
ATOM   2768 O  OE1  . GLU   B 1 81  ? -16.873 70.634 14.585  1.00 72.17 ? 112 GLU   B OE1  1 
ATOM   2769 O  OE2  . GLU   B 1 81  ? -15.501 68.927 14.575  1.00 61.73 ? 112 GLU   B OE2  1 
ATOM   2770 N  N    . LEU   B 1 82  ? -19.824 65.614 11.726  1.00 43.93 ? 113 LEU   B N    1 
ATOM   2771 C  CA   . LEU   B 1 82  ? -20.210 64.689 10.665  1.00 44.18 ? 113 LEU   B CA   1 
ATOM   2772 C  C    . LEU   B 1 82  ? -21.710 64.751 10.405  1.00 44.31 ? 113 LEU   B C    1 
ATOM   2773 O  O    . LEU   B 1 82  ? -22.144 64.785 9.246   1.00 43.68 ? 113 LEU   B O    1 
ATOM   2774 C  CB   . LEU   B 1 82  ? -19.768 63.271 11.025  1.00 40.18 ? 113 LEU   B CB   1 
ATOM   2775 C  CG   . LEU   B 1 82  ? -19.994 62.143 10.009  1.00 42.91 ? 113 LEU   B CG   1 
ATOM   2776 C  CD1  . LEU   B 1 82  ? -19.541 62.531 8.600   1.00 38.37 ? 113 LEU   B CD1  1 
ATOM   2777 C  CD2  . LEU   B 1 82  ? -19.249 60.907 10.479  1.00 38.81 ? 113 LEU   B CD2  1 
ATOM   2778 N  N    . LEU   B 1 83  ? -22.517 64.809 11.471  1.00 41.76 ? 114 LEU   B N    1 
ATOM   2779 C  CA   . LEU   B 1 83  ? -23.963 64.918 11.300  1.00 39.84 ? 114 LEU   B CA   1 
ATOM   2780 C  C    . LEU   B 1 83  ? -24.338 66.186 10.548  1.00 44.25 ? 114 LEU   B C    1 
ATOM   2781 O  O    . LEU   B 1 83  ? -25.235 66.168 9.695   1.00 46.49 ? 114 LEU   B O    1 
ATOM   2782 C  CB   . LEU   B 1 83  ? -24.669 64.867 12.659  1.00 43.32 ? 114 LEU   B CB   1 
ATOM   2783 C  CG   . LEU   B 1 83  ? -24.622 63.497 13.343  1.00 44.49 ? 114 LEU   B CG   1 
ATOM   2784 C  CD1  . LEU   B 1 83  ? -25.366 63.515 14.683  1.00 43.76 ? 114 LEU   B CD1  1 
ATOM   2785 C  CD2  . LEU   B 1 83  ? -25.186 62.416 12.426  1.00 40.18 ? 114 LEU   B CD2  1 
ATOM   2786 N  N    . ASN   B 1 84  ? -23.656 67.298 10.835  1.00 43.08 ? 115 ASN   B N    1 
ATOM   2787 C  CA   . ASN   B 1 84  ? -23.931 68.529 10.095  1.00 43.65 ? 115 ASN   B CA   1 
ATOM   2788 C  C    . ASN   B 1 84  ? -23.645 68.364 8.605   1.00 40.09 ? 115 ASN   B C    1 
ATOM   2789 O  O    . ASN   B 1 84  ? -24.439 68.795 7.761   1.00 41.68 ? 115 ASN   B O    1 
ATOM   2790 C  CB   . ASN   B 1 84  ? -23.106 69.678 10.667  1.00 42.88 ? 115 ASN   B CB   1 
ATOM   2791 C  CG   . ASN   B 1 84  ? -23.748 70.290 11.888  1.00 55.80 ? 115 ASN   B CG   1 
ATOM   2792 O  OD1  . ASN   B 1 84  ? -24.905 69.992 12.213  1.00 58.41 ? 115 ASN   B OD1  1 
ATOM   2793 N  ND2  . ASN   B 1 84  ? -23.014 71.163 12.564  1.00 60.08 ? 115 ASN   B ND2  1 
ATOM   2794 N  N    . LEU   B 1 85  ? -22.512 67.747 8.267   1.00 41.58 ? 116 LEU   B N    1 
ATOM   2795 C  CA   . LEU   B 1 85  ? -22.171 67.540 6.860   1.00 44.90 ? 116 LEU   B CA   1 
ATOM   2796 C  C    . LEU   B 1 85  ? -23.220 66.680 6.162   1.00 40.04 ? 116 LEU   B C    1 
ATOM   2797 O  O    . LEU   B 1 85  ? -23.674 67.011 5.064   1.00 42.95 ? 116 LEU   B O    1 
ATOM   2798 C  CB   . LEU   B 1 85  ? -20.785 66.905 6.766   1.00 43.52 ? 116 LEU   B CB   1 
ATOM   2799 C  CG   . LEU   B 1 85  ? -20.167 66.552 5.414   1.00 43.92 ? 116 LEU   B CG   1 
ATOM   2800 C  CD1  . LEU   B 1 85  ? -20.102 67.772 4.477   1.00 39.14 ? 116 LEU   B CD1  1 
ATOM   2801 C  CD2  . LEU   B 1 85  ? -18.783 65.991 5.679   1.00 39.61 ? 116 LEU   B CD2  1 
ATOM   2802 N  N    . ILE   B 1 86  ? -23.647 65.592 6.812   1.00 39.15 ? 117 ILE   B N    1 
ATOM   2803 C  CA   . ILE   B 1 86  ? -24.657 64.705 6.239   1.00 38.76 ? 117 ILE   B CA   1 
ATOM   2804 C  C    . ILE   B 1 86  ? -25.952 65.460 5.976   1.00 40.95 ? 117 ILE   B C    1 
ATOM   2805 O  O    . ILE   B 1 86  ? -26.572 65.301 4.919   1.00 43.08 ? 117 ILE   B O    1 
ATOM   2806 C  CB   . ILE   B 1 86  ? -24.879 63.492 7.162   1.00 40.21 ? 117 ILE   B CB   1 
ATOM   2807 C  CG1  . ILE   B 1 86  ? -23.632 62.603 7.153   1.00 40.58 ? 117 ILE   B CG1  1 
ATOM   2808 C  CG2  . ILE   B 1 86  ? -26.114 62.713 6.723   1.00 41.17 ? 117 ILE   B CG2  1 
ATOM   2809 C  CD1  . ILE   B 1 86  ? -23.630 61.514 8.200   1.00 41.33 ? 117 ILE   B CD1  1 
ATOM   2810 N  N    . ASN   B 1 87  ? -26.373 66.304 6.924   1.00 43.39 ? 118 ASN   B N    1 
ATOM   2811 C  CA   . ASN   B 1 87  ? -27.613 67.060 6.757   1.00 41.09 ? 118 ASN   B CA   1 
ATOM   2812 C  C    . ASN   B 1 87  ? -27.515 68.054 5.600   1.00 44.48 ? 118 ASN   B C    1 
ATOM   2813 O  O    . ASN   B 1 87  ? -28.458 68.192 4.808   1.00 43.25 ? 118 ASN   B O    1 
ATOM   2814 C  CB   . ASN   B 1 87  ? -27.959 67.769 8.068   1.00 48.11 ? 118 ASN   B CB   1 
ATOM   2815 C  CG   . ASN   B 1 87  ? -29.209 68.634 7.961   1.00 51.42 ? 118 ASN   B CG   1 
ATOM   2816 O  OD1  . ASN   B 1 87  ? -29.127 69.864 7.987   1.00 55.94 ? 118 ASN   B OD1  1 
ATOM   2817 N  ND2  . ASN   B 1 87  ? -30.369 67.996 7.838   1.00 49.82 ? 118 ASN   B ND2  1 
ATOM   2818 N  N    . LYS   B 1 88  ? -26.379 68.751 5.477   1.00 43.84 ? 119 LYS   B N    1 
ATOM   2819 C  CA   . LYS   B 1 88  ? -26.203 69.656 4.340   1.00 43.16 ? 119 LYS   B CA   1 
ATOM   2820 C  C    . LYS   B 1 88  ? -26.307 68.896 3.025   1.00 43.39 ? 119 LYS   B C    1 
ATOM   2821 O  O    . LYS   B 1 88  ? -26.977 69.348 2.090   1.00 43.82 ? 119 LYS   B O    1 
ATOM   2822 C  CB   . LYS   B 1 88  ? -24.858 70.376 4.433   1.00 45.32 ? 119 LYS   B CB   1 
ATOM   2823 C  CG   . LYS   B 1 88  ? -24.601 71.347 3.281   1.00 48.01 ? 119 LYS   B CG   1 
ATOM   2824 C  CD   . LYS   B 1 88  ? -23.202 71.952 3.358   1.00 50.74 ? 119 LYS   B CD   1 
ATOM   2825 C  CE   . LYS   B 1 88  ? -22.172 71.037 2.729   1.00 51.15 ? 119 LYS   B CE   1 
ATOM   2826 N  NZ   . LYS   B 1 88  ? -20.776 71.521 2.935   1.00 60.23 ? 119 LYS   B NZ   1 
ATOM   2827 N  N    . LEU   B 1 89  ? -25.680 67.715 2.952   1.00 41.77 ? 120 LEU   B N    1 
ATOM   2828 C  CA   . LEU   B 1 89  ? -25.710 66.925 1.723   1.00 43.08 ? 120 LEU   B CA   1 
ATOM   2829 C  C    . LEU   B 1 89  ? -27.092 66.329 1.463   1.00 43.55 ? 120 LEU   B C    1 
ATOM   2830 O  O    . LEU   B 1 89  ? -27.525 66.248 0.306   1.00 42.17 ? 120 LEU   B O    1 
ATOM   2831 C  CB   . LEU   B 1 89  ? -24.638 65.838 1.783   1.00 37.27 ? 120 LEU   B CB   1 
ATOM   2832 C  CG   . LEU   B 1 89  ? -23.216 66.405 1.694   1.00 40.80 ? 120 LEU   B CG   1 
ATOM   2833 C  CD1  . LEU   B 1 89  ? -22.178 65.315 1.874   1.00 44.66 ? 120 LEU   B CD1  1 
ATOM   2834 C  CD2  . LEU   B 1 89  ? -23.004 67.138 0.367   1.00 44.89 ? 120 LEU   B CD2  1 
ATOM   2835 N  N    . ASN   B 1 90  ? -27.805 65.921 2.519   1.00 44.04 ? 121 ASN   B N    1 
ATOM   2836 C  CA   . ASN   B 1 90  ? -29.183 65.453 2.359   1.00 43.36 ? 121 ASN   B CA   1 
ATOM   2837 C  C    . ASN   B 1 90  ? -30.061 66.501 1.682   1.00 45.55 ? 121 ASN   B C    1 
ATOM   2838 O  O    . ASN   B 1 90  ? -30.984 66.157 0.928   1.00 46.70 ? 121 ASN   B O    1 
ATOM   2839 C  CB   . ASN   B 1 90  ? -29.790 65.102 3.723   1.00 43.89 ? 121 ASN   B CB   1 
ATOM   2840 C  CG   . ASN   B 1 90  ? -29.320 63.758 4.269   1.00 45.10 ? 121 ASN   B CG   1 
ATOM   2841 O  OD1  . ASN   B 1 90  ? -28.956 62.855 3.511   1.00 41.68 ? 121 ASN   B OD1  1 
ATOM   2842 N  ND2  . ASN   B 1 90  ? -29.356 63.609 5.607   1.00 39.23 ? 121 ASN   B ND2  1 
ATOM   2843 N  N    . ASN   B 1 91  ? -29.805 67.776 1.957   1.00 48.27 ? 122 ASN   B N    1 
ATOM   2844 C  CA   . ASN   B 1 91  ? -30.618 68.878 1.464   1.00 48.45 ? 122 ASN   B CA   1 
ATOM   2845 C  C    . ASN   B 1 91  ? -30.067 69.489 0.191   1.00 53.36 ? 122 ASN   B C    1 
ATOM   2846 O  O    . ASN   B 1 91  ? -30.657 70.442 -0.330  1.00 57.06 ? 122 ASN   B O    1 
ATOM   2847 C  CB   . ASN   B 1 91  ? -30.746 69.956 2.543   1.00 54.80 ? 122 ASN   B CB   1 
ATOM   2848 C  CG   . ASN   B 1 91  ? -31.502 69.464 3.756   1.00 51.93 ? 122 ASN   B CG   1 
ATOM   2849 O  OD1  . ASN   B 1 91  ? -32.634 68.993 3.644   1.00 54.45 ? 122 ASN   B OD1  1 
ATOM   2850 N  ND2  . ASN   B 1 91  ? -30.873 69.547 4.918   1.00 53.27 ? 122 ASN   B ND2  1 
ATOM   2851 N  N    . ASP   B 1 92  ? -28.964 68.957 -0.323  1.00 51.93 ? 123 ASP   B N    1 
ATOM   2852 C  CA   . ASP   B 1 92  ? -28.411 69.377 -1.601  1.00 48.13 ? 123 ASP   B CA   1 
ATOM   2853 C  C    . ASP   B 1 92  ? -29.114 68.570 -2.683  1.00 51.00 ? 123 ASP   B C    1 
ATOM   2854 O  O    . ASP   B 1 92  ? -28.834 67.379 -2.857  1.00 49.47 ? 123 ASP   B O    1 
ATOM   2855 C  CB   . ASP   B 1 92  ? -26.901 69.156 -1.620  1.00 48.91 ? 123 ASP   B CB   1 
ATOM   2856 C  CG   . ASP   B 1 92  ? -26.235 69.737 -2.855  1.00 52.85 ? 123 ASP   B CG   1 
ATOM   2857 O  OD1  . ASP   B 1 92  ? -26.954 70.034 -3.836  1.00 51.05 ? 123 ASP   B OD1  1 
ATOM   2858 O  OD2  . ASP   B 1 92  ? -24.990 69.875 -2.845  1.00 50.76 ? 123 ASP   B OD2  1 
ATOM   2859 N  N    . ASP   B 1 93  ? -30.023 69.219 -3.415  1.00 52.68 ? 124 ASP   B N    1 
ATOM   2860 C  CA   . ASP   B 1 93  ? -30.776 68.529 -4.457  1.00 53.92 ? 124 ASP   B CA   1 
ATOM   2861 C  C    . ASP   B 1 93  ? -29.887 67.968 -5.560  1.00 49.75 ? 124 ASP   B C    1 
ATOM   2862 O  O    . ASP   B 1 93  ? -30.332 67.091 -6.307  1.00 51.37 ? 124 ASP   B O    1 
ATOM   2863 C  CB   . ASP   B 1 93  ? -31.809 69.467 -5.069  1.00 61.67 ? 124 ASP   B CB   1 
ATOM   2864 C  CG   . ASP   B 1 93  ? -32.993 69.689 -4.163  1.00 67.09 ? 124 ASP   B CG   1 
ATOM   2865 O  OD1  . ASP   B 1 93  ? -33.720 68.713 -3.885  1.00 70.93 ? 124 ASP   B OD1  1 
ATOM   2866 O  OD2  . ASP   B 1 93  ? -33.184 70.838 -3.716  1.00 71.28 ? 124 ASP   B OD2  1 
ATOM   2867 N  N    . ASN   B 1 94  ? -28.654 68.458 -5.701  1.00 48.79 ? 125 ASN   B N    1 
ATOM   2868 C  CA   . ASN   B 1 94  ? -27.776 67.895 -6.722  1.00 50.78 ? 125 ASN   B CA   1 
ATOM   2869 C  C    . ASN   B 1 94  ? -27.268 66.509 -6.344  1.00 48.49 ? 125 ASN   B C    1 
ATOM   2870 O  O    . ASN   B 1 94  ? -26.887 65.736 -7.228  1.00 46.47 ? 125 ASN   B O    1 
ATOM   2871 C  CB   . ASN   B 1 94  ? -26.591 68.826 -6.984  1.00 49.51 ? 125 ASN   B CB   1 
ATOM   2872 C  CG   . ASN   B 1 94  ? -25.758 68.384 -8.171  1.00 57.70 ? 125 ASN   B CG   1 
ATOM   2873 O  OD1  . ASN   B 1 94  ? -26.273 67.781 -9.128  1.00 56.56 ? 125 ASN   B OD1  1 
ATOM   2874 N  ND2  . ASN   B 1 94  ? -24.458 68.678 -8.122  1.00 56.58 ? 125 ASN   B ND2  1 
ATOM   2875 N  N    . VAL   B 1 95  ? -27.272 66.171 -5.060  1.00 46.38 ? 126 VAL   B N    1 
ATOM   2876 C  CA   . VAL   B 1 95  ? -26.703 64.918 -4.579  1.00 42.89 ? 126 VAL   B CA   1 
ATOM   2877 C  C    . VAL   B 1 95  ? -27.774 63.839 -4.662  1.00 42.79 ? 126 VAL   B C    1 
ATOM   2878 O  O    . VAL   B 1 95  ? -28.808 63.934 -3.996  1.00 46.45 ? 126 VAL   B O    1 
ATOM   2879 C  CB   . VAL   B 1 95  ? -26.179 65.080 -3.140  1.00 42.85 ? 126 VAL   B CB   1 
ATOM   2880 C  CG1  . VAL   B 1 95  ? -25.599 63.767 -2.604  1.00 38.40 ? 126 VAL   B CG1  1 
ATOM   2881 C  CG2  . VAL   B 1 95  ? -25.145 66.200 -3.099  1.00 40.29 ? 126 VAL   B CG2  1 
ATOM   2882 N  N    . ASP   B 1 96  ? -27.532 62.811 -5.475  1.00 39.63 ? 127 ASP   B N    1 
ATOM   2883 C  CA   . ASP   B 1 96  ? -28.464 61.690 -5.573  1.00 39.99 ? 127 ASP   B CA   1 
ATOM   2884 C  C    . ASP   B 1 96  ? -28.117 60.569 -4.609  1.00 41.51 ? 127 ASP   B C    1 
ATOM   2885 O  O    . ASP   B 1 96  ? -29.013 59.971 -3.994  1.00 41.16 ? 127 ASP   B O    1 
ATOM   2886 C  CB   . ASP   B 1 96  ? -28.476 61.136 -6.998  1.00 40.68 ? 127 ASP   B CB   1 
ATOM   2887 C  CG   . ASP   B 1 96  ? -28.821 62.190 -8.010  1.00 43.01 ? 127 ASP   B CG   1 
ATOM   2888 O  OD1  . ASP   B 1 96  ? -29.980 62.639 -8.003  1.00 46.19 ? 127 ASP   B OD1  1 
ATOM   2889 O  OD2  . ASP   B 1 96  ? -27.923 62.600 -8.771  1.00 41.89 ? 127 ASP   B OD2  1 
ATOM   2890 N  N    . GLY   B 1 97  ? -26.836 60.263 -4.492  1.00 38.54 ? 128 GLY   B N    1 
ATOM   2891 C  CA   . GLY   B 1 97  ? -26.364 59.221 -3.596  1.00 39.49 ? 128 GLY   B CA   1 
ATOM   2892 C  C    . GLY   B 1 97  ? -25.405 59.815 -2.584  1.00 37.14 ? 128 GLY   B C    1 
ATOM   2893 O  O    . GLY   B 1 97  ? -24.607 60.699 -2.918  1.00 39.18 ? 128 GLY   B O    1 
ATOM   2894 N  N    . LEU   B 1 98  ? -25.492 59.326 -1.350  1.00 37.54 ? 129 LEU   B N    1 
ATOM   2895 C  CA   . LEU   B 1 98  ? -24.632 59.770 -0.260  1.00 36.29 ? 129 LEU   B CA   1 
ATOM   2896 C  C    . LEU   B 1 98  ? -24.230 58.555 0.557   1.00 36.66 ? 129 LEU   B C    1 
ATOM   2897 O  O    . LEU   B 1 98  ? -25.092 57.770 0.963   1.00 35.92 ? 129 LEU   B O    1 
ATOM   2898 C  CB   . LEU   B 1 98  ? -25.347 60.792 0.632   1.00 35.72 ? 129 LEU   B CB   1 
ATOM   2899 C  CG   . LEU   B 1 98  ? -24.576 61.211 1.887   1.00 42.08 ? 129 LEU   B CG   1 
ATOM   2900 C  CD1  . LEU   B 1 98  ? -23.237 61.878 1.517   1.00 37.02 ? 129 LEU   B CD1  1 
ATOM   2901 C  CD2  . LEU   B 1 98  ? -25.451 62.113 2.757   1.00 38.92 ? 129 LEU   B CD2  1 
ATOM   2902 N  N    . LEU   B 1 99  ? -22.931 58.395 0.802   1.00 35.17 ? 130 LEU   B N    1 
ATOM   2903 C  CA   . LEU   B 1 99  ? -22.469 57.285 1.620   1.00 37.58 ? 130 LEU   B CA   1 
ATOM   2904 C  C    . LEU   B 1 99  ? -21.292 57.734 2.465   1.00 36.38 ? 130 LEU   B C    1 
ATOM   2905 O  O    . LEU   B 1 99  ? -20.477 58.561 2.039   1.00 34.93 ? 130 LEU   B O    1 
ATOM   2906 C  CB   . LEU   B 1 99  ? -22.076 56.069 0.763   1.00 37.15 ? 130 LEU   B CB   1 
ATOM   2907 C  CG   . LEU   B 1 99  ? -20.723 55.948 0.057   1.00 36.08 ? 130 LEU   B CG   1 
ATOM   2908 C  CD1  . LEU   B 1 99  ? -19.671 55.326 0.971   1.00 32.90 ? 130 LEU   B CD1  1 
ATOM   2909 C  CD2  . LEU   B 1 99  ? -20.910 55.069 -1.189  1.00 38.01 ? 130 LEU   B CD2  1 
ATOM   2910 N  N    . VAL   B 1 100 ? -21.206 57.166 3.662   1.00 36.36 ? 131 VAL   B N    1 
ATOM   2911 C  CA   . VAL   B 1 100 ? -20.116 57.427 4.586   1.00 31.96 ? 131 VAL   B CA   1 
ATOM   2912 C  C    . VAL   B 1 100 ? -19.276 56.161 4.658   1.00 35.08 ? 131 VAL   B C    1 
ATOM   2913 O  O    . VAL   B 1 100 ? -19.754 55.119 5.120   1.00 35.15 ? 131 VAL   B O    1 
ATOM   2914 C  CB   . VAL   B 1 100 ? -20.641 57.838 5.967   1.00 34.43 ? 131 VAL   B CB   1 
ATOM   2915 C  CG1  . VAL   B 1 100 ? -19.496 58.240 6.843   1.00 34.02 ? 131 VAL   B CG1  1 
ATOM   2916 C  CG2  . VAL   B 1 100 ? -21.652 58.980 5.819   1.00 33.99 ? 131 VAL   B CG2  1 
ATOM   2917 N  N    . GLN   B 1 101 ? -18.033 56.236 4.182   1.00 33.73 ? 132 GLN   B N    1 
ATOM   2918 C  CA   . GLN   B 1 101 ? -17.173 55.060 4.169   1.00 34.67 ? 132 GLN   B CA   1 
ATOM   2919 C  C    . GLN   B 1 101 ? -16.872 54.618 5.601   1.00 38.97 ? 132 GLN   B C    1 
ATOM   2920 O  O    . GLN   B 1 101 ? -16.595 55.447 6.475   1.00 35.46 ? 132 GLN   B O    1 
ATOM   2921 C  CB   . GLN   B 1 101 ? -15.869 55.369 3.431   1.00 34.71 ? 132 GLN   B CB   1 
ATOM   2922 C  CG   . GLN   B 1 101 ? -14.980 54.165 3.210   1.00 33.00 ? 132 GLN   B CG   1 
ATOM   2923 C  CD   . GLN   B 1 101 ? -15.522 53.259 2.121   1.00 33.85 ? 132 GLN   B CD   1 
ATOM   2924 O  OE1  . GLN   B 1 101 ? -16.365 53.668 1.310   1.00 32.40 ? 132 GLN   B OE1  1 
ATOM   2925 N  NE2  . GLN   B 1 101 ? -15.040 52.019 2.091   1.00 34.47 ? 132 GLN   B NE2  1 
ATOM   2926 N  N    . LEU   B 1 102 ? -16.925 53.305 5.838   1.00 37.09 ? 133 LEU   B N    1 
ATOM   2927 C  CA   . LEU   B 1 102 ? -16.658 52.695 7.139   1.00 36.89 ? 133 LEU   B CA   1 
ATOM   2928 C  C    . LEU   B 1 102 ? -15.342 51.933 7.076   1.00 38.44 ? 133 LEU   B C    1 
ATOM   2929 O  O    . LEU   B 1 102 ? -14.921 51.503 5.992   1.00 35.60 ? 133 LEU   B O    1 
ATOM   2930 C  CB   . LEU   B 1 102 ? -17.790 51.735 7.540   1.00 35.46 ? 133 LEU   B CB   1 
ATOM   2931 C  CG   . LEU   B 1 102 ? -19.203 52.332 7.571   1.00 37.23 ? 133 LEU   B CG   1 
ATOM   2932 C  CD1  . LEU   B 1 102 ? -20.296 51.278 7.860   1.00 35.34 ? 133 LEU   B CD1  1 
ATOM   2933 C  CD2  . LEU   B 1 102 ? -19.273 53.453 8.587   1.00 37.78 ? 133 LEU   B CD2  1 
ATOM   2934 N  N    . PRO   B 1 103 ? -14.659 51.727 8.220   1.00 34.74 ? 134 PRO   B N    1 
ATOM   2935 C  CA   . PRO   B 1 103 ? -15.042 52.079 9.596   1.00 39.92 ? 134 PRO   B CA   1 
ATOM   2936 C  C    . PRO   B 1 103 ? -14.827 53.551 9.932   1.00 40.40 ? 134 PRO   B C    1 
ATOM   2937 O  O    . PRO   B 1 103 ? -13.978 54.203 9.331   1.00 40.69 ? 134 PRO   B O    1 
ATOM   2938 C  CB   . PRO   B 1 103 ? -14.112 51.202 10.447  1.00 40.48 ? 134 PRO   B CB   1 
ATOM   2939 C  CG   . PRO   B 1 103 ? -12.872 51.116 9.631   1.00 41.54 ? 134 PRO   B CG   1 
ATOM   2940 C  CD   . PRO   B 1 103 ? -13.344 51.054 8.179   1.00 36.76 ? 134 PRO   B CD   1 
ATOM   2941 N  N    . LEU   B 1 104 ? -15.583 54.048 10.890  1.00 43.89 ? 135 LEU   B N    1 
ATOM   2942 C  CA   . LEU   B 1 104 ? -15.451 55.373 11.477  1.00 44.11 ? 135 LEU   B CA   1 
ATOM   2943 C  C    . LEU   B 1 104 ? -14.616 55.308 12.754  1.00 45.96 ? 135 LEU   B C    1 
ATOM   2944 O  O    . LEU   B 1 104 ? -14.397 54.226 13.308  1.00 40.68 ? 135 LEU   B O    1 
ATOM   2945 C  CB   . LEU   B 1 104 ? -16.840 55.950 11.782  1.00 41.28 ? 135 LEU   B CB   1 
ATOM   2946 C  CG   . LEU   B 1 104 ? -17.632 56.292 10.530  1.00 38.45 ? 135 LEU   B CG   1 
ATOM   2947 C  CD1  . LEU   B 1 104 ? -19.035 56.763 10.864  1.00 36.57 ? 135 LEU   B CD1  1 
ATOM   2948 C  CD2  . LEU   B 1 104 ? -16.867 57.344 9.714   1.00 38.77 ? 135 LEU   B CD2  1 
ATOM   2949 N  N    . PRO   B 1 105 ? -14.102 56.443 13.236  1.00 46.98 ? 136 PRO   B N    1 
ATOM   2950 C  CA   . PRO   B 1 105 ? -13.364 56.434 14.507  1.00 47.79 ? 136 PRO   B CA   1 
ATOM   2951 C  C    . PRO   B 1 105 ? -14.253 56.005 15.670  1.00 48.10 ? 136 PRO   B C    1 
ATOM   2952 O  O    . PRO   B 1 105 ? -15.477 56.145 15.639  1.00 47.00 ? 136 PRO   B O    1 
ATOM   2953 C  CB   . PRO   B 1 105 ? -12.904 57.890 14.664  1.00 45.64 ? 136 PRO   B CB   1 
ATOM   2954 C  CG   . PRO   B 1 105 ? -12.887 58.438 13.260  1.00 48.08 ? 136 PRO   B CG   1 
ATOM   2955 C  CD   . PRO   B 1 105 ? -14.064 57.772 12.593  1.00 46.33 ? 136 PRO   B CD   1 
ATOM   2956 N  N    . GLU   B 1 106 ? -13.602 55.478 16.715  1.00 48.79 ? 137 GLU   B N    1 
ATOM   2957 C  CA   . GLU   B 1 106 ? -14.321 54.837 17.816  1.00 48.44 ? 137 GLU   B CA   1 
ATOM   2958 C  C    . GLU   B 1 106 ? -15.295 55.785 18.506  1.00 48.00 ? 137 GLU   B C    1 
ATOM   2959 O  O    . GLU   B 1 106 ? -16.335 55.345 19.006  1.00 54.51 ? 137 GLU   B O    1 
ATOM   2960 C  CB   . GLU   B 1 106 ? -13.326 54.271 18.833  1.00 47.73 ? 137 GLU   B CB   1 
ATOM   2961 N  N    . HIS   B 1 107 ? -14.991 57.079 18.544  1.00 47.88 ? 138 HIS   B N    1 
ATOM   2962 C  CA   . HIS   B 1 107 ? -15.849 58.023 19.250  1.00 47.25 ? 138 HIS   B CA   1 
ATOM   2963 C  C    . HIS   B 1 107 ? -17.095 58.410 18.467  1.00 47.16 ? 138 HIS   B C    1 
ATOM   2964 O  O    . HIS   B 1 107 ? -17.886 59.225 18.952  1.00 46.07 ? 138 HIS   B O    1 
ATOM   2965 C  CB   . HIS   B 1 107 ? -15.061 59.283 19.610  1.00 47.05 ? 138 HIS   B CB   1 
ATOM   2966 C  CG   . HIS   B 1 107 ? -14.649 60.107 18.426  1.00 49.31 ? 138 HIS   B CG   1 
ATOM   2967 N  ND1  . HIS   B 1 107 ? -13.570 59.781 17.628  1.00 46.53 ? 138 HIS   B ND1  1 
ATOM   2968 C  CD2  . HIS   B 1 107 ? -15.159 61.256 17.920  1.00 44.48 ? 138 HIS   B CD2  1 
ATOM   2969 C  CE1  . HIS   B 1 107 ? -13.434 60.693 16.681  1.00 44.99 ? 138 HIS   B CE1  1 
ATOM   2970 N  NE2  . HIS   B 1 107 ? -14.384 61.600 16.838  1.00 43.90 ? 138 HIS   B NE2  1 
ATOM   2971 N  N    . ILE   B 1 108 ? -17.290 57.868 17.269  1.00 45.62 ? 139 ILE   B N    1 
ATOM   2972 C  CA   . ILE   B 1 108 ? -18.464 58.156 16.456  1.00 46.78 ? 139 ILE   B CA   1 
ATOM   2973 C  C    . ILE   B 1 108 ? -19.287 56.880 16.350  1.00 45.23 ? 139 ILE   B C    1 
ATOM   2974 O  O    . ILE   B 1 108 ? -18.751 55.814 16.025  1.00 47.99 ? 139 ILE   B O    1 
ATOM   2975 C  CB   . ILE   B 1 108 ? -18.058 58.679 15.064  1.00 48.95 ? 139 ILE   B CB   1 
ATOM   2976 C  CG1  . ILE   B 1 108 ? -17.278 59.995 15.202  1.00 46.62 ? 139 ILE   B CG1  1 
ATOM   2977 C  CG2  . ILE   B 1 108 ? -19.279 58.830 14.157  1.00 43.40 ? 139 ILE   B CG2  1 
ATOM   2978 C  CD1  . ILE   B 1 108 ? -16.896 60.625 13.877  1.00 46.57 ? 139 ILE   B CD1  1 
ATOM   2979 N  N    . ASP   B 1 109 ? -20.585 56.989 16.617  1.00 45.41 ? 140 ASP   B N    1 
ATOM   2980 C  CA   . ASP   B 1 109 ? -21.487 55.844 16.545  1.00 48.63 ? 140 ASP   B CA   1 
ATOM   2981 C  C    . ASP   B 1 109 ? -21.885 55.602 15.089  1.00 45.74 ? 140 ASP   B C    1 
ATOM   2982 O  O    . ASP   B 1 109 ? -22.635 56.391 14.509  1.00 43.36 ? 140 ASP   B O    1 
ATOM   2983 C  CB   . ASP   B 1 109 ? -22.711 56.095 17.423  1.00 50.30 ? 140 ASP   B CB   1 
ATOM   2984 C  CG   . ASP   B 1 109 ? -23.605 54.868 17.553  1.00 53.12 ? 140 ASP   B CG   1 
ATOM   2985 O  OD1  . ASP   B 1 109 ? -24.428 54.619 16.650  1.00 55.45 ? 140 ASP   B OD1  1 
ATOM   2986 O  OD2  . ASP   B 1 109 ? -23.472 54.138 18.557  1.00 62.88 ? 140 ASP   B OD2  1 
ATOM   2987 N  N    . GLU   B 1 110 ? -21.409 54.496 14.504  1.00 45.38 ? 141 GLU   B N    1 
ATOM   2988 C  CA   . GLU   B 1 110 ? -21.661 54.247 13.084  1.00 46.59 ? 141 GLU   B CA   1 
ATOM   2989 C  C    . GLU   B 1 110 ? -23.148 54.102 12.790  1.00 46.42 ? 141 GLU   B C    1 
ATOM   2990 O  O    . GLU   B 1 110 ? -23.618 54.552 11.740  1.00 42.21 ? 141 GLU   B O    1 
ATOM   2991 C  CB   . GLU   B 1 110 ? -20.896 53.011 12.608  1.00 45.92 ? 141 GLU   B CB   1 
ATOM   2992 C  CG   . GLU   B 1 110 ? -19.389 53.240 12.585  1.00 47.34 ? 141 GLU   B CG   1 
ATOM   2993 C  CD   . GLU   B 1 110 ? -18.598 52.048 12.081  1.00 49.90 ? 141 GLU   B CD   1 
ATOM   2994 O  OE1  . GLU   B 1 110 ? -19.208 51.027 11.667  1.00 50.54 ? 141 GLU   B OE1  1 
ATOM   2995 O  OE2  . GLU   B 1 110 ? -17.351 52.146 12.100  1.00 45.94 ? 141 GLU   B OE2  1 
ATOM   2996 N  N    . ARG   B 1 111 ? -23.909 53.479 13.700  1.00 44.75 ? 142 ARG   B N    1 
ATOM   2997 C  CA   . ARG   B 1 111 ? -25.342 53.323 13.460  1.00 44.76 ? 142 ARG   B CA   1 
ATOM   2998 C  C    . ARG   B 1 111 ? -26.059 54.668 13.427  1.00 43.69 ? 142 ARG   B C    1 
ATOM   2999 O  O    . ARG   B 1 111 ? -26.979 54.856 12.627  1.00 44.35 ? 142 ARG   B O    1 
ATOM   3000 C  CB   . ARG   B 1 111 ? -25.990 52.412 14.511  1.00 49.54 ? 142 ARG   B CB   1 
ATOM   3001 C  CG   . ARG   B 1 111 ? -25.751 50.904 14.344  1.00 46.94 ? 142 ARG   B CG   1 
ATOM   3002 C  CD   . ARG   B 1 111 ? -25.980 50.375 12.943  1.00 50.68 ? 142 ARG   B CD   1 
ATOM   3003 N  NE   . ARG   B 1 111 ? -27.154 50.949 12.298  1.00 51.12 ? 142 ARG   B NE   1 
ATOM   3004 C  CZ   . ARG   B 1 111 ? -27.396 50.871 10.996  1.00 47.11 ? 142 ARG   B CZ   1 
ATOM   3005 N  NH1  . ARG   B 1 111 ? -26.582 50.215 10.179  1.00 54.27 ? 142 ARG   B NH1  1 
ATOM   3006 N  NH2  . ARG   B 1 111 ? -28.483 51.461 10.496  1.00 39.65 ? 142 ARG   B NH2  1 
ATOM   3007 N  N    . ARG   B 1 112 ? -25.694 55.602 14.319  1.00 46.85 ? 143 ARG   B N    1 
ATOM   3008 C  CA   . ARG   B 1 112 ? -26.299 56.934 14.254  1.00 45.09 ? 143 ARG   B CA   1 
ATOM   3009 C  C    . ARG   B 1 112 ? -25.950 57.626 12.939  1.00 43.16 ? 143 ARG   B C    1 
ATOM   3010 O  O    . ARG   B 1 112 ? -26.804 58.276 12.320  1.00 41.04 ? 143 ARG   B O    1 
ATOM   3011 C  CB   . ARG   B 1 112 ? -25.870 57.787 15.455  1.00 49.07 ? 143 ARG   B CB   1 
ATOM   3012 C  CG   . ARG   B 1 112 ? -26.715 57.523 16.716  1.00 57.99 ? 143 ARG   B CG   1 
ATOM   3013 C  CD   . ARG   B 1 112 ? -26.394 58.447 17.907  1.00 61.91 ? 143 ARG   B CD   1 
ATOM   3014 N  NE   . ARG   B 1 112 ? -25.093 58.167 18.506  1.00 62.22 ? 143 ARG   B NE   1 
ATOM   3015 C  CZ   . ARG   B 1 112 ? -24.801 58.346 19.788  1.00 67.27 ? 143 ARG   B CZ   1 
ATOM   3016 N  NH1  . ARG   B 1 112 ? -25.712 58.767 20.652  1.00 73.47 ? 143 ARG   B NH1  1 
ATOM   3017 N  NH2  . ARG   B 1 112 ? -23.566 58.087 20.216  1.00 66.44 ? 143 ARG   B NH2  1 
ATOM   3018 N  N    . ILE   B 1 113 ? -24.709 57.468 12.476  1.00 42.43 ? 144 ILE   B N    1 
ATOM   3019 C  CA   . ILE   B 1 113 ? -24.317 58.072 11.200  1.00 40.95 ? 144 ILE   B CA   1 
ATOM   3020 C  C    . ILE   B 1 113 ? -25.098 57.455 10.044  1.00 40.23 ? 144 ILE   B C    1 
ATOM   3021 O  O    . ILE   B 1 113 ? -25.667 58.169 9.213   1.00 41.66 ? 144 ILE   B O    1 
ATOM   3022 C  CB   . ILE   B 1 113 ? -22.802 57.939 10.996  1.00 40.72 ? 144 ILE   B CB   1 
ATOM   3023 C  CG1  . ILE   B 1 113 ? -22.075 58.657 12.135  1.00 42.25 ? 144 ILE   B CG1  1 
ATOM   3024 C  CG2  . ILE   B 1 113 ? -22.397 58.476 9.608   1.00 37.34 ? 144 ILE   B CG2  1 
ATOM   3025 C  CD1  . ILE   B 1 113 ? -22.434 60.114 12.271  1.00 37.64 ? 144 ILE   B CD1  1 
ATOM   3026 N  N    . CYS   B 1 114 ? -25.158 56.119 9.983   1.00 42.70 ? 145 CYS   B N    1 
ATOM   3027 C  CA   . CYS   B 1 114 ? -25.831 55.472 8.853   1.00 41.80 ? 145 CYS   B CA   1 
ATOM   3028 C  C    . CYS   B 1 114 ? -27.306 55.850 8.782   1.00 42.69 ? 145 CYS   B C    1 
ATOM   3029 O  O    . CYS   B 1 114 ? -27.864 55.955 7.685   1.00 41.36 ? 145 CYS   B O    1 
ATOM   3030 C  CB   . CYS   B 1 114 ? -25.676 53.948 8.940   1.00 40.28 ? 145 CYS   B CB   1 
ATOM   3031 S  SG   . CYS   B 1 114 ? -23.949 53.366 8.855   1.00 49.71 ? 145 CYS   B SG   1 
ATOM   3032 N  N    . ASN   B 1 115 ? -27.955 56.062 9.932   1.00 37.91 ? 146 ASN   B N    1 
ATOM   3033 C  CA   . ASN   B 1 115 ? -29.361 56.459 9.939   1.00 39.06 ? 146 ASN   B CA   1 
ATOM   3034 C  C    . ASN   B 1 115 ? -29.561 57.938 9.645   1.00 39.57 ? 146 ASN   B C    1 
ATOM   3035 O  O    . ASN   B 1 115 ? -30.689 58.350 9.350   1.00 40.51 ? 146 ASN   B O    1 
ATOM   3036 C  CB   . ASN   B 1 115 ? -30.008 56.118 11.291  1.00 43.89 ? 146 ASN   B CB   1 
ATOM   3037 C  CG   . ASN   B 1 115 ? -30.162 54.634 11.485  1.00 45.57 ? 146 ASN   B CG   1 
ATOM   3038 O  OD1  . ASN   B 1 115 ? -30.304 53.896 10.505  1.00 40.65 ? 146 ASN   B OD1  1 
ATOM   3039 N  ND2  . ASN   B 1 115 ? -30.092 54.175 12.738  1.00 42.51 ? 146 ASN   B ND2  1 
ATOM   3040 N  N    . ALA   B 1 116 ? -28.504 58.744 9.727   1.00 39.44 ? 147 ALA   B N    1 
ATOM   3041 C  CA   . ALA   B 1 116 ? -28.613 60.154 9.380   1.00 43.50 ? 147 ALA   B CA   1 
ATOM   3042 C  C    . ALA   B 1 116 ? -28.647 60.387 7.871   1.00 39.02 ? 147 ALA   B C    1 
ATOM   3043 O  O    . ALA   B 1 116 ? -29.111 61.444 7.431   1.00 39.46 ? 147 ALA   B O    1 
ATOM   3044 C  CB   . ALA   B 1 116 ? -27.455 60.936 10.006  1.00 40.24 ? 147 ALA   B CB   1 
ATOM   3045 N  N    . VAL   B 1 117 ? -28.165 59.440 7.064   1.00 40.73 ? 148 VAL   B N    1 
ATOM   3046 C  CA   . VAL   B 1 117 ? -28.258 59.593 5.614   1.00 36.06 ? 148 VAL   B CA   1 
ATOM   3047 C  C    . VAL   B 1 117 ? -29.710 59.424 5.199   1.00 39.03 ? 148 VAL   B C    1 
ATOM   3048 O  O    . VAL   B 1 117 ? -30.387 58.478 5.625   1.00 44.10 ? 148 VAL   B O    1 
ATOM   3049 C  CB   . VAL   B 1 117 ? -27.354 58.576 4.899   1.00 43.30 ? 148 VAL   B CB   1 
ATOM   3050 C  CG1  . VAL   B 1 117 ? -27.450 58.738 3.380   1.00 39.24 ? 148 VAL   B CG1  1 
ATOM   3051 C  CG2  . VAL   B 1 117 ? -25.914 58.720 5.371   1.00 39.23 ? 148 VAL   B CG2  1 
ATOM   3052 N  N    . SER   B 1 118 ? -30.203 60.342 4.385   1.00 39.77 ? 149 SER   B N    1 
ATOM   3053 C  CA   . SER   B 1 118 ? -31.573 60.239 3.916   1.00 43.00 ? 149 SER   B CA   1 
ATOM   3054 C  C    . SER   B 1 118 ? -31.776 58.891 3.229   1.00 44.64 ? 149 SER   B C    1 
ATOM   3055 O  O    . SER   B 1 118 ? -30.960 58.512 2.372   1.00 44.54 ? 149 SER   B O    1 
ATOM   3056 C  CB   . SER   B 1 118 ? -31.898 61.369 2.945   1.00 47.00 ? 149 SER   B CB   1 
ATOM   3057 O  OG   . SER   B 1 118 ? -33.060 61.046 2.205   1.00 53.01 ? 149 SER   B OG   1 
ATOM   3058 N  N    . PRO   B 1 119 ? -32.825 58.139 3.586   1.00 45.66 ? 150 PRO   B N    1 
ATOM   3059 C  CA   . PRO   B 1 119 ? -32.994 56.793 3.014   1.00 44.69 ? 150 PRO   B CA   1 
ATOM   3060 C  C    . PRO   B 1 119 ? -33.044 56.785 1.495   1.00 44.73 ? 150 PRO   B C    1 
ATOM   3061 O  O    . PRO   B 1 119 ? -32.646 55.789 0.880   1.00 45.37 ? 150 PRO   B O    1 
ATOM   3062 C  CB   . PRO   B 1 119 ? -34.318 56.318 3.632   1.00 42.22 ? 150 PRO   B CB   1 
ATOM   3063 C  CG   . PRO   B 1 119 ? -34.425 57.083 4.915   1.00 44.14 ? 150 PRO   B CG   1 
ATOM   3064 C  CD   . PRO   B 1 119 ? -33.826 58.428 4.632   1.00 46.95 ? 150 PRO   B CD   1 
ATOM   3065 N  N    . ASP   B 1 120 ? -33.506 57.869 0.868   1.00 45.92 ? 151 ASP   B N    1 
ATOM   3066 C  CA   . ASP   B 1 120 ? -33.551 57.921 -0.589  1.00 46.27 ? 151 ASP   B CA   1 
ATOM   3067 C  C    . ASP   B 1 120 ? -32.177 58.135 -1.218  1.00 47.61 ? 151 ASP   B C    1 
ATOM   3068 O  O    . ASP   B 1 120 ? -32.017 57.879 -2.418  1.00 40.19 ? 151 ASP   B O    1 
ATOM   3069 C  CB   . ASP   B 1 120 ? -34.509 59.025 -1.045  1.00 47.19 ? 151 ASP   B CB   1 
ATOM   3070 C  CG   . ASP   B 1 120 ? -35.953 58.750 -0.635  1.00 58.25 ? 151 ASP   B CG   1 
ATOM   3071 O  OD1  . ASP   B 1 120 ? -36.405 57.586 -0.745  1.00 62.17 ? 151 ASP   B OD1  1 
ATOM   3072 O  OD2  . ASP   B 1 120 ? -36.636 59.695 -0.190  1.00 62.84 ? 151 ASP   B OD2  1 
ATOM   3073 N  N    . LYS   B 1 121 ? -31.191 58.603 -0.445  1.00 44.54 ? 152 LYS   B N    1 
ATOM   3074 C  CA   . LYS   B 1 121 ? -29.818 58.760 -0.920  1.00 41.04 ? 152 LYS   B CA   1 
ATOM   3075 C  C    . LYS   B 1 121 ? -28.896 57.658 -0.416  1.00 39.43 ? 152 LYS   B C    1 
ATOM   3076 O  O    . LYS   B 1 121 ? -27.708 57.653 -0.762  1.00 37.49 ? 152 LYS   B O    1 
ATOM   3077 C  CB   . LYS   B 1 121 ? -29.268 60.138 -0.517  1.00 41.61 ? 152 LYS   B CB   1 
ATOM   3078 C  CG   . LYS   B 1 121 ? -30.152 61.307 -1.001  1.00 45.31 ? 152 LYS   B CG   1 
ATOM   3079 C  CD   . LYS   B 1 121 ? -29.477 62.668 -0.864  1.00 43.45 ? 152 LYS   B CD   1 
ATOM   3080 C  CE   . LYS   B 1 121 ? -30.404 63.804 -1.310  1.00 42.91 ? 152 LYS   B CE   1 
ATOM   3081 N  NZ   . LYS   B 1 121 ? -29.703 65.139 -1.297  1.00 42.59 ? 152 LYS   B NZ   1 
ATOM   3082 N  N    . ASP   B 1 122 ? -29.439 56.697 0.336   1.00 35.98 ? 153 ASP   B N    1 
ATOM   3083 C  CA   . ASP   B 1 122 ? -28.683 55.671 1.058   1.00 39.51 ? 153 ASP   B CA   1 
ATOM   3084 C  C    . ASP   B 1 122 ? -28.286 54.539 0.105   1.00 38.41 ? 153 ASP   B C    1 
ATOM   3085 O  O    . ASP   B 1 122 ? -28.772 53.410 0.183   1.00 38.01 ? 153 ASP   B O    1 
ATOM   3086 C  CB   . ASP   B 1 122 ? -29.521 55.168 2.232   1.00 37.22 ? 153 ASP   B CB   1 
ATOM   3087 C  CG   . ASP   B 1 122 ? -28.867 54.036 3.009   1.00 39.60 ? 153 ASP   B CG   1 
ATOM   3088 O  OD1  . ASP   B 1 122 ? -29.608 53.136 3.476   1.00 36.15 ? 153 ASP   B OD1  1 
ATOM   3089 O  OD2  . ASP   B 1 122 ? -27.624 54.039 3.155   1.00 37.07 ? 153 ASP   B OD2  1 
ATOM   3090 N  N    . VAL   B 1 123 ? -27.339 54.850 -0.786  1.00 36.54 ? 154 VAL   B N    1 
ATOM   3091 C  CA   . VAL   B 1 123 ? -26.900 53.852 -1.763  1.00 37.85 ? 154 VAL   B CA   1 
ATOM   3092 C  C    . VAL   B 1 123 ? -26.208 52.663 -1.092  1.00 37.77 ? 154 VAL   B C    1 
ATOM   3093 O  O    . VAL   B 1 123 ? -26.038 51.615 -1.730  1.00 39.11 ? 154 VAL   B O    1 
ATOM   3094 C  CB   . VAL   B 1 123 ? -25.987 54.494 -2.827  1.00 34.13 ? 154 VAL   B CB   1 
ATOM   3095 C  CG1  . VAL   B 1 123 ? -26.787 55.476 -3.690  1.00 33.64 ? 154 VAL   B CG1  1 
ATOM   3096 C  CG2  . VAL   B 1 123 ? -24.804 55.208 -2.170  1.00 33.15 ? 154 VAL   B CG2  1 
ATOM   3097 N  N    . ASP   B 1 124 ? -25.793 52.799 0.176   1.00 31.12 ? 155 ASP   B N    1 
ATOM   3098 C  CA   . ASP   B 1 124 ? -25.260 51.664 0.921   1.00 33.39 ? 155 ASP   B CA   1 
ATOM   3099 C  C    . ASP   B 1 124 ? -26.345 50.679 1.357   1.00 34.11 ? 155 ASP   B C    1 
ATOM   3100 O  O    . ASP   B 1 124 ? -26.030 49.521 1.654   1.00 35.89 ? 155 ASP   B O    1 
ATOM   3101 C  CB   . ASP   B 1 124 ? -24.523 52.140 2.179   1.00 35.18 ? 155 ASP   B CB   1 
ATOM   3102 C  CG   . ASP   B 1 124 ? -23.053 52.426 1.947   1.00 38.97 ? 155 ASP   B CG   1 
ATOM   3103 O  OD1  . ASP   B 1 124 ? -22.415 51.775 1.087   1.00 37.17 ? 155 ASP   B OD1  1 
ATOM   3104 O  OD2  . ASP   B 1 124 ? -22.526 53.298 2.677   1.00 41.47 ? 155 ASP   B OD2  1 
ATOM   3105 N  N    . GLY   B 1 125 ? -27.598 51.114 1.448   1.00 33.23 ? 156 GLY   B N    1 
ATOM   3106 C  CA   . GLY   B 1 125 ? -28.600 50.284 2.098   1.00 35.29 ? 156 GLY   B CA   1 
ATOM   3107 C  C    . GLY   B 1 125 ? -28.336 50.039 3.571   1.00 35.96 ? 156 GLY   B C    1 
ATOM   3108 O  O    . GLY   B 1 125 ? -28.705 48.980 4.090   1.00 36.38 ? 156 GLY   B O    1 
ATOM   3109 N  N    . PHE   B 1 126 ? -27.686 50.982 4.262   1.00 34.84 ? 157 PHE   B N    1 
ATOM   3110 C  CA   . PHE   B 1 126 ? -27.365 50.818 5.679   1.00 34.76 ? 157 PHE   B CA   1 
ATOM   3111 C  C    . PHE   B 1 126 ? -28.377 51.483 6.614   1.00 39.05 ? 157 PHE   B C    1 
ATOM   3112 O  O    . PHE   B 1 126 ? -28.353 51.219 7.825   1.00 39.87 ? 157 PHE   B O    1 
ATOM   3113 C  CB   . PHE   B 1 126 ? -25.970 51.387 5.980   1.00 37.52 ? 157 PHE   B CB   1 
ATOM   3114 C  CG   . PHE   B 1 126 ? -24.825 50.582 5.395   1.00 39.10 ? 157 PHE   B CG   1 
ATOM   3115 C  CD1  . PHE   B 1 126 ? -25.033 49.313 4.867   1.00 35.42 ? 157 PHE   B CD1  1 
ATOM   3116 C  CD2  . PHE   B 1 126 ? -23.533 51.099 5.407   1.00 34.64 ? 157 PHE   B CD2  1 
ATOM   3117 C  CE1  . PHE   B 1 126 ? -23.980 48.578 4.356   1.00 38.71 ? 157 PHE   B CE1  1 
ATOM   3118 C  CE2  . PHE   B 1 126 ? -22.479 50.384 4.892   1.00 35.37 ? 157 PHE   B CE2  1 
ATOM   3119 C  CZ   . PHE   B 1 126 ? -22.700 49.108 4.359   1.00 35.92 ? 157 PHE   B CZ   1 
ATOM   3120 N  N    . HIS   B 1 127 ? -29.253 52.337 6.096   1.00 39.52 ? 158 HIS   B N    1 
ATOM   3121 C  CA   . HIS   B 1 127 ? -30.267 52.966 6.933   1.00 40.50 ? 158 HIS   B CA   1 
ATOM   3122 C  C    . HIS   B 1 127 ? -31.263 51.918 7.426   1.00 40.68 ? 158 HIS   B C    1 
ATOM   3123 O  O    . HIS   B 1 127 ? -31.638 51.003 6.689   1.00 37.98 ? 158 HIS   B O    1 
ATOM   3124 C  CB   . HIS   B 1 127 ? -30.976 54.066 6.145   1.00 38.67 ? 158 HIS   B CB   1 
ATOM   3125 C  CG   . HIS   B 1 127 ? -31.918 54.910 6.951   1.00 44.33 ? 158 HIS   B CG   1 
ATOM   3126 N  ND1  . HIS   B 1 127 ? -33.117 54.433 7.441   1.00 43.71 ? 158 HIS   B ND1  1 
ATOM   3127 C  CD2  . HIS   B 1 127 ? -31.866 56.220 7.296   1.00 43.21 ? 158 HIS   B CD2  1 
ATOM   3128 C  CE1  . HIS   B 1 127 ? -33.746 55.405 8.081   1.00 46.26 ? 158 HIS   B CE1  1 
ATOM   3129 N  NE2  . HIS   B 1 127 ? -33.009 56.499 8.008   1.00 40.69 ? 158 HIS   B NE2  1 
ATOM   3130 N  N    . VAL   B 1 128 ? -31.712 52.076 8.679   1.00 40.17 ? 159 VAL   B N    1 
ATOM   3131 C  CA   . VAL   B 1 128 ? -32.484 51.023 9.341   1.00 36.91 ? 159 VAL   B CA   1 
ATOM   3132 C  C    . VAL   B 1 128 ? -33.744 50.680 8.546   1.00 37.80 ? 159 VAL   B C    1 
ATOM   3133 O  O    . VAL   B 1 128 ? -34.151 49.513 8.476   1.00 36.57 ? 159 VAL   B O    1 
ATOM   3134 C  CB   . VAL   B 1 128 ? -32.805 51.430 10.795  1.00 42.25 ? 159 VAL   B CB   1 
ATOM   3135 C  CG1  . VAL   B 1 128 ? -33.748 52.639 10.843  1.00 38.09 ? 159 VAL   B CG1  1 
ATOM   3136 C  CG2  . VAL   B 1 128 ? -33.371 50.244 11.552  1.00 35.45 ? 159 VAL   B CG2  1 
ATOM   3137 N  N    . ILE   B 1 129 ? -34.365 51.675 7.912   1.00 38.33 ? 160 ILE   B N    1 
ATOM   3138 C  CA   . ILE   B 1 129 ? -35.508 51.402 7.041   1.00 40.62 ? 160 ILE   B CA   1 
ATOM   3139 C  C    . ILE   B 1 129 ? -35.098 50.523 5.860   1.00 43.29 ? 160 ILE   B C    1 
ATOM   3140 O  O    . ILE   B 1 129 ? -35.842 49.621 5.445   1.00 38.32 ? 160 ILE   B O    1 
ATOM   3141 C  CB   . ILE   B 1 129 ? -36.138 52.724 6.571   1.00 43.39 ? 160 ILE   B CB   1 
ATOM   3142 C  CG1  . ILE   B 1 129 ? -36.927 53.368 7.714   1.00 44.15 ? 160 ILE   B CG1  1 
ATOM   3143 C  CG2  . ILE   B 1 129 ? -37.023 52.496 5.369   1.00 42.63 ? 160 ILE   B CG2  1 
ATOM   3144 C  CD1  . ILE   B 1 129 ? -37.214 54.841 7.502   1.00 49.89 ? 160 ILE   B CD1  1 
ATOM   3145 N  N    . ASN   B 1 130 ? -33.925 50.785 5.279   1.00 40.84 ? 161 ASN   B N    1 
ATOM   3146 C  CA   . ASN   B 1 130 ? -33.460 49.942 4.179   1.00 37.56 ? 161 ASN   B CA   1 
ATOM   3147 C  C    . ASN   B 1 130 ? -33.107 48.543 4.671   1.00 33.69 ? 161 ASN   B C    1 
ATOM   3148 O  O    . ASN   B 1 130 ? -33.385 47.554 3.988   1.00 34.44 ? 161 ASN   B O    1 
ATOM   3149 C  CB   . ASN   B 1 130 ? -32.256 50.585 3.493   1.00 36.32 ? 161 ASN   B CB   1 
ATOM   3150 C  CG   . ASN   B 1 130 ? -32.653 51.507 2.363   1.00 46.75 ? 161 ASN   B CG   1 
ATOM   3151 O  OD1  . ASN   B 1 130 ? -33.377 51.105 1.439   1.00 49.45 ? 161 ASN   B OD1  1 
ATOM   3152 N  ND2  . ASN   B 1 130 ? -32.183 52.752 2.422   1.00 42.84 ? 161 ASN   B ND2  1 
ATOM   3153 N  N    . VAL   B 1 131 ? -32.512 48.440 5.863   1.00 35.16 ? 162 VAL   B N    1 
ATOM   3154 C  CA   . VAL   B 1 131 ? -32.229 47.124 6.442   1.00 35.53 ? 162 VAL   B CA   1 
ATOM   3155 C  C    . VAL   B 1 131 ? -33.527 46.362 6.674   1.00 38.05 ? 162 VAL   B C    1 
ATOM   3156 O  O    . VAL   B 1 131 ? -33.666 45.197 6.277   1.00 32.29 ? 162 VAL   B O    1 
ATOM   3157 C  CB   . VAL   B 1 131 ? -31.430 47.258 7.752   1.00 35.12 ? 162 VAL   B CB   1 
ATOM   3158 C  CG1  . VAL   B 1 131 ? -31.279 45.901 8.370   1.00 31.66 ? 162 VAL   B CG1  1 
ATOM   3159 C  CG2  . VAL   B 1 131 ? -30.060 47.872 7.500   1.00 37.38 ? 162 VAL   B CG2  1 
ATOM   3160 N  N    . GLY   B 1 132 ? -34.502 47.017 7.314   1.00 35.44 ? 163 GLY   B N    1 
ATOM   3161 C  CA   . GLY   B 1 132 ? -35.786 46.369 7.551   1.00 33.32 ? 163 GLY   B CA   1 
ATOM   3162 C  C    . GLY   B 1 132 ? -36.475 45.937 6.267   1.00 33.33 ? 163 GLY   B C    1 
ATOM   3163 O  O    . GLY   B 1 132 ? -36.939 44.799 6.147   1.00 30.66 ? 163 GLY   B O    1 
ATOM   3164 N  N    . ARG   B 1 133 ? -36.532 46.834 5.280   1.00 34.54 ? 164 ARG   B N    1 
ATOM   3165 C  CA   . ARG   B 1 133 ? -37.161 46.492 4.005   1.00 35.79 ? 164 ARG   B CA   1 
ATOM   3166 C  C    . ARG   B 1 133 ? -36.468 45.304 3.347   1.00 34.56 ? 164 ARG   B C    1 
ATOM   3167 O  O    . ARG   B 1 133 ? -37.132 44.387 2.847   1.00 38.43 ? 164 ARG   B O    1 
ATOM   3168 C  CB   . ARG   B 1 133 ? -37.169 47.712 3.075   1.00 36.45 ? 164 ARG   B CB   1 
ATOM   3169 C  CG   . ARG   B 1 133 ? -38.208 48.760 3.478   1.00 37.91 ? 164 ARG   B CG   1 
ATOM   3170 C  CD   . ARG   B 1 133 ? -38.219 49.968 2.566   1.00 42.30 ? 164 ARG   B CD   1 
ATOM   3171 N  NE   . ARG   B 1 133 ? -38.612 49.587 1.219   1.00 47.96 ? 164 ARG   B NE   1 
ATOM   3172 C  CZ   . ARG   B 1 133 ? -39.867 49.521 0.797   1.00 47.71 ? 164 ARG   B CZ   1 
ATOM   3173 N  NH1  . ARG   B 1 133 ? -40.878 49.854 1.583   1.00 47.85 ? 164 ARG   B NH1  1 
ATOM   3174 N  NH2  . ARG   B 1 133 ? -40.115 49.099 -0.440  1.00 39.89 ? 164 ARG   B NH2  1 
ATOM   3175 N  N    . MET   B 1 134 ? -35.132 45.291 3.358   1.00 32.64 ? 165 MET   B N    1 
ATOM   3176 C  CA   . MET   B 1 134 ? -34.397 44.146 2.831   1.00 35.90 ? 165 MET   B CA   1 
ATOM   3177 C  C    . MET   B 1 134 ? -34.775 42.862 3.554   1.00 36.82 ? 165 MET   B C    1 
ATOM   3178 O  O    . MET   B 1 134 ? -35.010 41.823 2.925   1.00 32.47 ? 165 MET   B O    1 
ATOM   3179 C  CB   . MET   B 1 134 ? -32.893 44.376 2.963   1.00 36.86 ? 165 MET   B CB   1 
ATOM   3180 C  CG   . MET   B 1 134 ? -32.100 43.167 2.533   1.00 42.87 ? 165 MET   B CG   1 
ATOM   3181 S  SD   . MET   B 1 134 ? -30.382 43.190 3.023   1.00 53.48 ? 165 MET   B SD   1 
ATOM   3182 C  CE   . MET   B 1 134 ? -30.418 42.015 4.372   1.00 45.68 ? 165 MET   B CE   1 
ATOM   3183 N  N    . CYS   B 1 135 ? -34.836 42.909 4.882   1.00 33.55 ? 166 CYS   B N    1 
ATOM   3184 C  CA   . CYS   B 1 135 ? -35.101 41.699 5.641   1.00 32.67 ? 166 CYS   B CA   1 
ATOM   3185 C  C    . CYS   B 1 135 ? -36.537 41.233 5.463   1.00 31.69 ? 166 CYS   B C    1 
ATOM   3186 O  O    . CYS   B 1 135 ? -36.834 40.065 5.734   1.00 35.79 ? 166 CYS   B O    1 
ATOM   3187 C  CB   . CYS   B 1 135 ? -34.752 41.937 7.120   1.00 34.20 ? 166 CYS   B CB   1 
ATOM   3188 S  SG   . CYS   B 1 135 ? -32.939 42.101 7.368   1.00 41.40 ? 166 CYS   B SG   1 
ATOM   3189 N  N    . LEU   B 1 136 ? -37.418 42.104 4.973   1.00 30.84 ? 167 LEU   B N    1 
ATOM   3190 C  CA   . LEU   B 1 136 ? -38.781 41.736 4.593   1.00 32.79 ? 167 LEU   B CA   1 
ATOM   3191 C  C    . LEU   B 1 136 ? -38.923 41.386 3.103   1.00 35.73 ? 167 LEU   B C    1 
ATOM   3192 O  O    . LEU   B 1 136 ? -40.055 41.264 2.610   1.00 32.25 ? 167 LEU   B O    1 
ATOM   3193 C  CB   . LEU   B 1 136 ? -39.741 42.870 4.953   1.00 29.20 ? 167 LEU   B CB   1 
ATOM   3194 C  CG   . LEU   B 1 136 ? -39.720 43.144 6.457   1.00 32.38 ? 167 LEU   B CG   1 
ATOM   3195 C  CD1  . LEU   B 1 136 ? -40.549 44.371 6.819   1.00 32.16 ? 167 LEU   B CD1  1 
ATOM   3196 C  CD2  . LEU   B 1 136 ? -40.226 41.890 7.146   1.00 31.64 ? 167 LEU   B CD2  1 
ATOM   3197 N  N    . ASP   B 1 137 ? -37.809 41.244 2.377   1.00 34.85 ? 168 ASP   B N    1 
ATOM   3198 C  CA   . ASP   B 1 137 ? -37.827 40.942 0.938   1.00 34.84 ? 168 ASP   B CA   1 
ATOM   3199 C  C    . ASP   B 1 137 ? -38.586 41.998 0.140   1.00 37.32 ? 168 ASP   B C    1 
ATOM   3200 O  O    . ASP   B 1 137 ? -39.177 41.695 -0.904  1.00 41.20 ? 168 ASP   B O    1 
ATOM   3201 C  CB   . ASP   B 1 137 ? -38.422 39.557 0.636   1.00 36.60 ? 168 ASP   B CB   1 
ATOM   3202 C  CG   . ASP   B 1 137 ? -37.678 38.418 1.319   1.00 34.95 ? 168 ASP   B CG   1 
ATOM   3203 O  OD1  . ASP   B 1 137 ? -36.528 38.600 1.785   1.00 32.53 ? 168 ASP   B OD1  1 
ATOM   3204 O  OD2  . ASP   B 1 137 ? -38.250 37.309 1.365   1.00 33.94 ? 168 ASP   B OD2  1 
ATOM   3205 N  N    . GLN   B 1 138 ? -38.571 43.245 0.596   1.00 34.85 ? 169 GLN   B N    1 
ATOM   3206 C  CA   . GLN   B 1 138 ? -39.210 44.330 -0.134  1.00 39.51 ? 169 GLN   B CA   1 
ATOM   3207 C  C    . GLN   B 1 138 ? -38.194 45.049 -1.024  1.00 38.82 ? 169 GLN   B C    1 
ATOM   3208 O  O    . GLN   B 1 138 ? -36.981 45.011 -0.778  1.00 34.28 ? 169 GLN   B O    1 
ATOM   3209 C  CB   . GLN   B 1 138 ? -39.845 45.337 0.827   1.00 36.59 ? 169 GLN   B CB   1 
ATOM   3210 C  CG   . GLN   B 1 138 ? -40.965 44.802 1.714   1.00 38.99 ? 169 GLN   B CG   1 
ATOM   3211 C  CD   . GLN   B 1 138 ? -41.460 45.870 2.672   1.00 42.48 ? 169 GLN   B CD   1 
ATOM   3212 O  OE1  . GLN   B 1 138 ? -40.785 46.202 3.644   1.00 40.13 ? 169 GLN   B OE1  1 
ATOM   3213 N  NE2  . GLN   B 1 138 ? -42.627 46.442 2.380   1.00 47.67 ? 169 GLN   B NE2  1 
ATOM   3214 N  N    . TYR   B 1 139 ? -38.708 45.722 -2.060  1.00 38.49 ? 170 TYR   B N    1 
ATOM   3215 C  CA   . TYR   B 1 139 ? -37.864 46.603 -2.866  1.00 39.30 ? 170 TYR   B CA   1 
ATOM   3216 C  C    . TYR   B 1 139 ? -37.024 47.484 -1.958  1.00 40.54 ? 170 TYR   B C    1 
ATOM   3217 O  O    . TYR   B 1 139 ? -37.552 48.184 -1.088  1.00 41.00 ? 170 TYR   B O    1 
ATOM   3218 C  CB   . TYR   B 1 139 ? -38.713 47.483 -3.787  1.00 41.41 ? 170 TYR   B CB   1 
ATOM   3219 C  CG   . TYR   B 1 139 ? -39.494 46.738 -4.833  1.00 46.18 ? 170 TYR   B CG   1 
ATOM   3220 C  CD1  . TYR   B 1 139 ? -38.878 45.806 -5.664  1.00 50.45 ? 170 TYR   B CD1  1 
ATOM   3221 C  CD2  . TYR   B 1 139 ? -40.857 46.968 -4.993  1.00 52.16 ? 170 TYR   B CD2  1 
ATOM   3222 C  CE1  . TYR   B 1 139 ? -39.603 45.121 -6.635  1.00 53.13 ? 170 TYR   B CE1  1 
ATOM   3223 C  CE2  . TYR   B 1 139 ? -41.591 46.290 -5.958  1.00 56.70 ? 170 TYR   B CE2  1 
ATOM   3224 C  CZ   . TYR   B 1 139 ? -40.959 45.369 -6.775  1.00 54.40 ? 170 TYR   B CZ   1 
ATOM   3225 O  OH   . TYR   B 1 139 ? -41.693 44.695 -7.726  1.00 65.68 ? 170 TYR   B OH   1 
ATOM   3226 N  N    . SER   B 1 140 ? -35.713 47.424 -2.136  1.00 38.96 ? 171 SER   B N    1 
ATOM   3227 C  CA   . SER   B 1 140 ? -34.819 48.201 -1.295  1.00 39.05 ? 171 SER   B CA   1 
ATOM   3228 C  C    . SER   B 1 140 ? -33.513 48.407 -2.041  1.00 40.79 ? 171 SER   B C    1 
ATOM   3229 O  O    . SER   B 1 140 ? -33.212 47.715 -3.017  1.00 36.06 ? 171 SER   B O    1 
ATOM   3230 C  CB   . SER   B 1 140 ? -34.556 47.505 0.044   1.00 37.06 ? 171 SER   B CB   1 
ATOM   3231 O  OG   . SER   B 1 140 ? -33.691 46.406 -0.168  1.00 40.07 ? 171 SER   B OG   1 
ATOM   3232 N  N    . MET   B 1 141 ? -32.738 49.367 -1.547  1.00 38.84 ? 172 MET   B N    1 
ATOM   3233 C  CA   . MET   B 1 141 ? -31.361 49.564 -1.970  1.00 38.74 ? 172 MET   B CA   1 
ATOM   3234 C  C    . MET   B 1 141 ? -30.524 48.488 -1.295  1.00 42.08 ? 172 MET   B C    1 
ATOM   3235 O  O    . MET   B 1 141 ? -30.328 48.528 -0.074  1.00 39.11 ? 172 MET   B O    1 
ATOM   3236 C  CB   . MET   B 1 141 ? -30.879 50.950 -1.553  1.00 39.78 ? 172 MET   B CB   1 
ATOM   3237 C  CG   . MET   B 1 141 ? -29.715 51.452 -2.365  1.00 48.24 ? 172 MET   B CG   1 
ATOM   3238 S  SD   . MET   B 1 141 ? -30.307 52.343 -3.803  1.00 54.45 ? 172 MET   B SD   1 
ATOM   3239 C  CE   . MET   B 1 141 ? -30.912 53.847 -3.067  1.00 42.17 ? 172 MET   B CE   1 
ATOM   3240 N  N    . LEU   B 1 142 ? -30.062 47.514 -2.071  1.00 36.01 ? 173 LEU   B N    1 
ATOM   3241 C  CA   . LEU   B 1 142 ? -29.293 46.404 -1.527  1.00 35.48 ? 173 LEU   B CA   1 
ATOM   3242 C  C    . LEU   B 1 142 ? -27.860 46.842 -1.230  1.00 39.50 ? 173 LEU   B C    1 
ATOM   3243 O  O    . LEU   B 1 142 ? -27.268 47.594 -2.005  1.00 38.64 ? 173 LEU   B O    1 
ATOM   3244 C  CB   . LEU   B 1 142 ? -29.289 45.233 -2.503  1.00 41.50 ? 173 LEU   B CB   1 
ATOM   3245 C  CG   . LEU   B 1 142 ? -30.678 44.683 -2.813  1.00 38.64 ? 173 LEU   B CG   1 
ATOM   3246 C  CD1  . LEU   B 1 142 ? -30.575 43.527 -3.779  1.00 36.39 ? 173 LEU   B CD1  1 
ATOM   3247 C  CD2  . LEU   B 1 142 ? -31.350 44.241 -1.500  1.00 41.07 ? 173 LEU   B CD2  1 
ATOM   3248 N  N    . PRO   B 1 143 ? -27.288 46.394 -0.113  1.00 34.85 ? 174 PRO   B N    1 
ATOM   3249 C  CA   . PRO   B 1 143 ? -25.885 46.722 0.166   1.00 36.37 ? 174 PRO   B CA   1 
ATOM   3250 C  C    . PRO   B 1 143 ? -24.974 46.150 -0.917  1.00 37.94 ? 174 PRO   B C    1 
ATOM   3251 O  O    . PRO   B 1 143 ? -25.214 45.063 -1.451  1.00 35.51 ? 174 PRO   B O    1 
ATOM   3252 C  CB   . PRO   B 1 143 ? -25.625 46.102 1.545   1.00 34.32 ? 174 PRO   B CB   1 
ATOM   3253 C  CG   . PRO   B 1 143 ? -26.838 45.317 1.917   1.00 39.89 ? 174 PRO   B CG   1 
ATOM   3254 C  CD   . PRO   B 1 143 ? -27.954 45.658 0.976   1.00 39.09 ? 174 PRO   B CD   1 
ATOM   3255 N  N    . ALA   B 1 144 ? -23.938 46.918 -1.267  1.00 36.94 ? 175 ALA   B N    1 
ATOM   3256 C  CA   . ALA   B 1 144 ? -23.175 46.621 -2.481  1.00 35.13 ? 175 ALA   B CA   1 
ATOM   3257 C  C    . ALA   B 1 144 ? -22.444 45.282 -2.389  1.00 33.76 ? 175 ALA   B C    1 
ATOM   3258 O  O    . ALA   B 1 144 ? -22.499 44.480 -3.325  1.00 37.01 ? 175 ALA   B O    1 
ATOM   3259 C  CB   . ALA   B 1 144 ? -22.190 47.752 -2.784  1.00 34.37 ? 175 ALA   B CB   1 
ATOM   3260 N  N    . THR   B 1 145 ? -21.732 45.020 -1.286  1.00 36.09 ? 176 THR   B N    1 
ATOM   3261 C  CA   . THR   B 1 145 ? -20.967 43.774 -1.246  1.00 35.65 ? 176 THR   B CA   1 
ATOM   3262 C  C    . THR   B 1 145 ? -21.869 42.551 -1.278  1.00 36.93 ? 176 THR   B C    1 
ATOM   3263 O  O    . THR   B 1 145 ? -21.623 41.657 -2.106  1.00 39.05 ? 176 THR   B O    1 
ATOM   3264 C  CB   . THR   B 1 145 ? -20.024 43.730 -0.042  1.00 37.54 ? 176 THR   B CB   1 
ATOM   3265 O  OG1  . THR   B 1 145 ? -19.080 44.797 -0.120  1.00 39.18 ? 176 THR   B OG1  1 
ATOM   3266 C  CG2  . THR   B 1 145 ? -19.286 42.393 -0.021  1.00 38.88 ? 176 THR   B CG2  1 
ATOM   3267 N  N    . PRO   B 1 146 ? -22.911 42.435 -0.436  1.00 38.58 ? 177 PRO   B N    1 
ATOM   3268 C  CA   . PRO   B 1 146 ? -23.828 41.296 -0.596  1.00 35.20 ? 177 PRO   B CA   1 
ATOM   3269 C  C    . PRO   B 1 146 ? -24.463 41.216 -1.971  1.00 37.63 ? 177 PRO   B C    1 
ATOM   3270 O  O    . PRO   B 1 146 ? -24.592 40.109 -2.504  1.00 37.92 ? 177 PRO   B O    1 
ATOM   3271 C  CB   . PRO   B 1 146 ? -24.864 41.533 0.515   1.00 39.76 ? 177 PRO   B CB   1 
ATOM   3272 C  CG   . PRO   B 1 146 ? -24.058 42.249 1.607   1.00 35.17 ? 177 PRO   B CG   1 
ATOM   3273 C  CD   . PRO   B 1 146 ? -23.200 43.193 0.805   1.00 34.93 ? 177 PRO   B CD   1 
ATOM   3274 N  N    . TRP   B 1 147 ? -24.850 42.345 -2.578  1.00 31.17 ? 178 TRP   B N    1 
ATOM   3275 C  CA   . TRP   B 1 147 ? -25.414 42.264 -3.922  1.00 37.32 ? 178 TRP   B CA   1 
ATOM   3276 C  C    . TRP   B 1 147 ? -24.379 41.746 -4.920  1.00 36.49 ? 178 TRP   B C    1 
ATOM   3277 O  O    . TRP   B 1 147 ? -24.687 40.885 -5.747  1.00 38.33 ? 178 TRP   B O    1 
ATOM   3278 C  CB   . TRP   B 1 147 ? -25.964 43.616 -4.368  1.00 34.33 ? 178 TRP   B CB   1 
ATOM   3279 C  CG   . TRP   B 1 147 ? -26.854 43.500 -5.535  1.00 38.48 ? 178 TRP   B CG   1 
ATOM   3280 C  CD1  . TRP   B 1 147 ? -27.295 42.344 -6.103  1.00 40.84 ? 178 TRP   B CD1  1 
ATOM   3281 C  CD2  . TRP   B 1 147 ? -27.411 44.568 -6.311  1.00 35.28 ? 178 TRP   B CD2  1 
ATOM   3282 N  NE1  . TRP   B 1 147 ? -28.092 42.621 -7.178  1.00 39.32 ? 178 TRP   B NE1  1 
ATOM   3283 C  CE2  . TRP   B 1 147 ? -28.179 43.980 -7.331  1.00 40.75 ? 178 TRP   B CE2  1 
ATOM   3284 C  CE3  . TRP   B 1 147 ? -27.328 45.964 -6.246  1.00 38.19 ? 178 TRP   B CE3  1 
ATOM   3285 C  CZ2  . TRP   B 1 147 ? -28.867 44.739 -8.287  1.00 38.78 ? 178 TRP   B CZ2  1 
ATOM   3286 C  CZ3  . TRP   B 1 147 ? -28.018 46.718 -7.178  1.00 35.13 ? 178 TRP   B CZ3  1 
ATOM   3287 C  CH2  . TRP   B 1 147 ? -28.771 46.105 -8.195  1.00 39.23 ? 178 TRP   B CH2  1 
ATOM   3288 N  N    . GLY   B 1 148 ? -23.138 42.228 -4.829  1.00 34.35 ? 179 GLY   B N    1 
ATOM   3289 C  CA   . GLY   B 1 148 ? -22.086 41.703 -5.690  1.00 39.26 ? 179 GLY   B CA   1 
ATOM   3290 C  C    . GLY   B 1 148 ? -21.897 40.202 -5.550  1.00 40.04 ? 179 GLY   B C    1 
ATOM   3291 O  O    . GLY   B 1 148 ? -21.683 39.502 -6.535  1.00 38.44 ? 179 GLY   B O    1 
ATOM   3292 N  N    . VAL   B 1 149 ? -21.982 39.683 -4.324  1.00 38.40 ? 180 VAL   B N    1 
ATOM   3293 C  CA   . VAL   B 1 149 ? -21.899 38.237 -4.135  1.00 35.48 ? 180 VAL   B CA   1 
ATOM   3294 C  C    . VAL   B 1 149 ? -23.045 37.552 -4.864  1.00 40.15 ? 180 VAL   B C    1 
ATOM   3295 O  O    . VAL   B 1 149 ? -22.846 36.595 -5.628  1.00 42.66 ? 180 VAL   B O    1 
ATOM   3296 C  CB   . VAL   B 1 149 ? -21.888 37.899 -2.630  1.00 36.75 ? 180 VAL   B CB   1 
ATOM   3297 C  CG1  . VAL   B 1 149 ? -22.127 36.416 -2.407  1.00 36.54 ? 180 VAL   B CG1  1 
ATOM   3298 C  CG2  . VAL   B 1 149 ? -20.575 38.319 -2.039  1.00 34.14 ? 180 VAL   B CG2  1 
ATOM   3299 N  N    . TRP   B 1 150 ? -24.257 38.077 -4.690  1.00 40.86 ? 181 TRP   B N    1 
ATOM   3300 C  CA   . TRP   B 1 150 ? -25.409 37.550 -5.409  1.00 41.47 ? 181 TRP   B CA   1 
ATOM   3301 C  C    . TRP   B 1 150 ? -25.170 37.551 -6.920  1.00 44.66 ? 181 TRP   B C    1 
ATOM   3302 O  O    . TRP   B 1 150 ? -25.427 36.549 -7.601  1.00 42.10 ? 181 TRP   B O    1 
ATOM   3303 C  CB   . TRP   B 1 150 ? -26.642 38.374 -5.052  1.00 40.92 ? 181 TRP   B CB   1 
ATOM   3304 C  CG   . TRP   B 1 150 ? -27.846 38.046 -5.862  1.00 50.98 ? 181 TRP   B CG   1 
ATOM   3305 C  CD1  . TRP   B 1 150 ? -28.220 38.612 -7.067  1.00 52.02 ? 181 TRP   B CD1  1 
ATOM   3306 C  CD2  . TRP   B 1 150 ? -28.852 37.085 -5.544  1.00 47.54 ? 181 TRP   B CD2  1 
ATOM   3307 N  NE1  . TRP   B 1 150 ? -29.394 38.043 -7.509  1.00 57.18 ? 181 TRP   B NE1  1 
ATOM   3308 C  CE2  . TRP   B 1 150 ? -29.802 37.107 -6.589  1.00 58.89 ? 181 TRP   B CE2  1 
ATOM   3309 C  CE3  . TRP   B 1 150 ? -29.034 36.197 -4.494  1.00 53.27 ? 181 TRP   B CE3  1 
ATOM   3310 C  CZ2  . TRP   B 1 150 ? -30.921 36.283 -6.591  1.00 53.60 ? 181 TRP   B CZ2  1 
ATOM   3311 C  CZ3  . TRP   B 1 150 ? -30.144 35.385 -4.502  1.00 55.40 ? 181 TRP   B CZ3  1 
ATOM   3312 C  CH2  . TRP   B 1 150 ? -31.068 35.428 -5.539  1.00 43.98 ? 181 TRP   B CH2  1 
ATOM   3313 N  N    . GLU   B 1 151 ? -24.690 38.675 -7.466  1.00 42.62 ? 182 GLU   B N    1 
ATOM   3314 C  CA   . GLU   B 1 151 ? -24.521 38.777 -8.917  1.00 43.20 ? 182 GLU   B CA   1 
ATOM   3315 C  C    . GLU   B 1 151 ? -23.457 37.818 -9.426  1.00 42.06 ? 182 GLU   B C    1 
ATOM   3316 O  O    . GLU   B 1 151 ? -23.593 37.265 -10.524 1.00 42.82 ? 182 GLU   B O    1 
ATOM   3317 C  CB   . GLU   B 1 151 ? -24.168 40.206 -9.326  1.00 43.91 ? 182 GLU   B CB   1 
ATOM   3318 C  CG   . GLU   B 1 151 ? -25.321 41.170 -9.268  1.00 44.82 ? 182 GLU   B CG   1 
ATOM   3319 C  CD   . GLU   B 1 151 ? -26.469 40.744 -10.136 1.00 47.62 ? 182 GLU   B CD   1 
ATOM   3320 O  OE1  . GLU   B 1 151 ? -26.215 40.151 -11.209 1.00 46.42 ? 182 GLU   B OE1  1 
ATOM   3321 O  OE2  . GLU   B 1 151 ? -27.628 41.006 -9.738  1.00 46.88 ? 182 GLU   B OE2  1 
ATOM   3322 N  N    . ILE   B 1 152 ? -22.377 37.636 -8.659  1.00 38.58 ? 183 ILE   B N    1 
ATOM   3323 C  CA   . ILE   B 1 152 ? -21.336 36.684 -9.035  1.00 41.57 ? 183 ILE   B CA   1 
ATOM   3324 C  C    . ILE   B 1 152 ? -21.948 35.311 -9.262  1.00 47.15 ? 183 ILE   B C    1 
ATOM   3325 O  O    . ILE   B 1 152 ? -21.671 34.636 -10.264 1.00 39.14 ? 183 ILE   B O    1 
ATOM   3326 C  CB   . ILE   B 1 152 ? -20.245 36.626 -7.953  1.00 42.85 ? 183 ILE   B CB   1 
ATOM   3327 C  CG1  . ILE   B 1 152 ? -19.218 37.737 -8.133  1.00 40.96 ? 183 ILE   B CG1  1 
ATOM   3328 C  CG2  . ILE   B 1 152 ? -19.558 35.256 -7.937  1.00 47.81 ? 183 ILE   B CG2  1 
ATOM   3329 C  CD1  . ILE   B 1 152 ? -18.239 37.812 -6.979  1.00 38.93 ? 183 ILE   B CD1  1 
ATOM   3330 N  N    . ILE   B 1 153 ? -22.804 34.889 -8.330  1.00 39.64 ? 184 ILE   B N    1 
ATOM   3331 C  CA   . ILE   B 1 153 ? -23.416 33.566 -8.394  1.00 42.31 ? 184 ILE   B CA   1 
ATOM   3332 C  C    . ILE   B 1 153 ? -24.394 33.484 -9.557  1.00 44.32 ? 184 ILE   B C    1 
ATOM   3333 O  O    . ILE   B 1 153 ? -24.345 32.550 -10.368 1.00 50.42 ? 184 ILE   B O    1 
ATOM   3334 C  CB   . ILE   B 1 153 ? -24.102 33.245 -7.048  1.00 41.39 ? 184 ILE   B CB   1 
ATOM   3335 C  CG1  . ILE   B 1 153 ? -23.047 33.069 -5.952  1.00 38.36 ? 184 ILE   B CG1  1 
ATOM   3336 C  CG2  . ILE   B 1 153 ? -25.008 32.027 -7.185  1.00 40.42 ? 184 ILE   B CG2  1 
ATOM   3337 C  CD1  . ILE   B 1 153 ? -23.589 33.152 -4.511  1.00 41.88 ? 184 ILE   B CD1  1 
ATOM   3338 N  N    . LYS   B 1 154 ? -25.285 34.469 -9.670  1.00 40.13 ? 185 LYS   B N    1 
ATOM   3339 C  CA   . LYS   B 1 154 ? -26.302 34.419 -10.713 1.00 42.90 ? 185 LYS   B CA   1 
ATOM   3340 C  C    . LYS   B 1 154 ? -25.685 34.510 -12.102 1.00 48.59 ? 185 LYS   B C    1 
ATOM   3341 O  O    . LYS   B 1 154 ? -26.077 33.767 -13.011 1.00 45.52 ? 185 LYS   B O    1 
ATOM   3342 C  CB   . LYS   B 1 154 ? -27.320 35.541 -10.517 1.00 47.47 ? 185 LYS   B CB   1 
ATOM   3343 C  CG   . LYS   B 1 154 ? -28.242 35.322 -9.329  1.00 52.14 ? 185 LYS   B CG   1 
ATOM   3344 C  CD   . LYS   B 1 154 ? -28.670 33.862 -9.278  1.00 56.85 ? 185 LYS   B CD   1 
ATOM   3345 C  CE   . LYS   B 1 154 ? -29.627 33.555 -8.122  1.00 53.71 ? 185 LYS   B CE   1 
ATOM   3346 N  NZ   . LYS   B 1 154 ? -29.925 32.088 -8.124  1.00 49.65 ? 185 LYS   B NZ   1 
ATOM   3347 N  N    . ARG   B 1 155 ? -24.726 35.418 -12.291 1.00 45.24 ? 186 ARG   B N    1 
ATOM   3348 C  CA   . ARG   B 1 155 ? -24.199 35.645 -13.632 1.00 50.96 ? 186 ARG   B CA   1 
ATOM   3349 C  C    . ARG   B 1 155 ? -23.267 34.528 -14.077 1.00 49.68 ? 186 ARG   B C    1 
ATOM   3350 O  O    . ARG   B 1 155 ? -23.096 34.326 -15.279 1.00 48.93 ? 186 ARG   B O    1 
ATOM   3351 C  CB   . ARG   B 1 155 ? -23.499 37.009 -13.706 1.00 44.75 ? 186 ARG   B CB   1 
ATOM   3352 C  CG   . ARG   B 1 155 ? -24.501 38.171 -13.758 1.00 49.80 ? 186 ARG   B CG   1 
ATOM   3353 C  CD   . ARG   B 1 155 ? -23.848 39.554 -13.715 1.00 49.24 ? 186 ARG   B CD   1 
ATOM   3354 N  NE   . ARG   B 1 155 ? -24.848 40.618 -13.673 1.00 47.62 ? 186 ARG   B NE   1 
ATOM   3355 C  CZ   . ARG   B 1 155 ? -25.105 41.448 -14.676 1.00 50.72 ? 186 ARG   B CZ   1 
ATOM   3356 N  NH1  . ARG   B 1 155 ? -24.441 41.381 -15.816 1.00 49.64 ? 186 ARG   B NH1  1 
ATOM   3357 N  NH2  . ARG   B 1 155 ? -26.048 42.377 -14.531 1.00 48.61 ? 186 ARG   B NH2  1 
ATOM   3358 N  N    . THR   B 1 156 ? -22.670 33.798 -13.134 1.00 50.71 ? 187 THR   B N    1 
ATOM   3359 C  CA   . THR   B 1 156 ? -21.921 32.596 -13.463 1.00 50.53 ? 187 THR   B CA   1 
ATOM   3360 C  C    . THR   B 1 156 ? -22.834 31.400 -13.738 1.00 51.60 ? 187 THR   B C    1 
ATOM   3361 O  O    . THR   B 1 156 ? -22.355 30.364 -14.207 1.00 55.07 ? 187 THR   B O    1 
ATOM   3362 C  CB   . THR   B 1 156 ? -20.939 32.290 -12.326 1.00 46.18 ? 187 THR   B CB   1 
ATOM   3363 O  OG1  . THR   B 1 156 ? -20.148 33.458 -12.053 1.00 45.77 ? 187 THR   B OG1  1 
ATOM   3364 C  CG2  . THR   B 1 156 ? -20.009 31.133 -12.674 1.00 52.02 ? 187 THR   B CG2  1 
ATOM   3365 N  N    . GLY   B 1 157 ? -24.139 31.526 -13.498 1.00 48.94 ? 188 GLY   B N    1 
ATOM   3366 C  CA   . GLY   B 1 157 ? -25.063 30.434 -13.750 1.00 47.82 ? 188 GLY   B CA   1 
ATOM   3367 C  C    . GLY   B 1 157 ? -25.094 29.352 -12.693 1.00 54.24 ? 188 GLY   B C    1 
ATOM   3368 O  O    . GLY   B 1 157 ? -25.581 28.251 -12.965 1.00 54.71 ? 188 GLY   B O    1 
ATOM   3369 N  N    . ILE   B 1 158 ? -24.582 29.625 -11.497 1.00 49.51 ? 189 ILE   B N    1 
ATOM   3370 C  CA   . ILE   B 1 158 ? -24.572 28.664 -10.397 1.00 52.36 ? 189 ILE   B CA   1 
ATOM   3371 C  C    . ILE   B 1 158 ? -25.948 28.636 -9.741  1.00 53.69 ? 189 ILE   B C    1 
ATOM   3372 O  O    . ILE   B 1 158 ? -26.396 29.663 -9.209  1.00 50.16 ? 189 ILE   B O    1 
ATOM   3373 C  CB   . ILE   B 1 158 ? -23.482 29.024 -9.380  1.00 47.68 ? 189 ILE   B CB   1 
ATOM   3374 C  CG1  . ILE   B 1 158 ? -22.119 29.049 -10.073 1.00 45.57 ? 189 ILE   B CG1  1 
ATOM   3375 C  CG2  . ILE   B 1 158 ? -23.521 28.065 -8.186  1.00 47.03 ? 189 ILE   B CG2  1 
ATOM   3376 C  CD1  . ILE   B 1 158 ? -21.040 29.732 -9.286  1.00 43.52 ? 189 ILE   B CD1  1 
ATOM   3377 N  N    . PRO   B 1 159 ? -26.656 27.506 -9.757  1.00 55.20 ? 190 PRO   B N    1 
ATOM   3378 C  CA   . PRO   B 1 159 ? -28.004 27.477 -9.172  1.00 48.94 ? 190 PRO   B CA   1 
ATOM   3379 C  C    . PRO   B 1 159 ? -27.983 27.608 -7.653  1.00 47.27 ? 190 PRO   B C    1 
ATOM   3380 O  O    . PRO   B 1 159 ? -27.038 27.190 -6.975  1.00 48.37 ? 190 PRO   B O    1 
ATOM   3381 C  CB   . PRO   B 1 159 ? -28.555 26.112 -9.601  1.00 49.90 ? 190 PRO   B CB   1 
ATOM   3382 C  CG   . PRO   B 1 159 ? -27.328 25.279 -9.906  1.00 58.77 ? 190 PRO   B CG   1 
ATOM   3383 C  CD   . PRO   B 1 159 ? -26.313 26.248 -10.446 1.00 54.40 ? 190 PRO   B CD   1 
ATOM   3384 N  N    . THR   B 1 160 ? -29.058 28.197 -7.124  1.00 47.84 ? 191 THR   B N    1 
ATOM   3385 C  CA   . THR   B 1 160 ? -29.247 28.343 -5.680  1.00 44.70 ? 191 THR   B CA   1 
ATOM   3386 C  C    . THR   B 1 160 ? -30.489 27.646 -5.144  1.00 42.03 ? 191 THR   B C    1 
ATOM   3387 O  O    . THR   B 1 160 ? -30.462 27.173 -4.009  1.00 44.06 ? 191 THR   B O    1 
ATOM   3388 C  CB   . THR   B 1 160 ? -29.319 29.833 -5.282  1.00 39.50 ? 191 THR   B CB   1 
ATOM   3389 O  OG1  . THR   B 1 160 ? -30.364 30.493 -6.020  1.00 41.16 ? 191 THR   B OG1  1 
ATOM   3390 C  CG2  . THR   B 1 160 ? -27.989 30.532 -5.528  1.00 44.42 ? 191 THR   B CG2  1 
ATOM   3391 N  N    . LEU   B 1 161 ? -31.572 27.569 -5.918  1.00 43.90 ? 192 LEU   B N    1 
ATOM   3392 C  CA   . LEU   B 1 161 ? -32.824 27.049 -5.385  1.00 43.22 ? 192 LEU   B CA   1 
ATOM   3393 C  C    . LEU   B 1 161 ? -32.651 25.612 -4.927  1.00 48.02 ? 192 LEU   B C    1 
ATOM   3394 O  O    . LEU   B 1 161 ? -32.317 24.735 -5.726  1.00 45.32 ? 192 LEU   B O    1 
ATOM   3395 C  CB   . LEU   B 1 161 ? -33.927 27.139 -6.432  1.00 42.58 ? 192 LEU   B CB   1 
ATOM   3396 C  CG   . LEU   B 1 161 ? -35.289 26.703 -5.906  1.00 45.67 ? 192 LEU   B CG   1 
ATOM   3397 C  CD1  . LEU   B 1 161 ? -36.353 27.648 -6.409  1.00 44.90 ? 192 LEU   B CD1  1 
ATOM   3398 C  CD2  . LEU   B 1 161 ? -35.610 25.262 -6.299  1.00 45.54 ? 192 LEU   B CD2  1 
ATOM   3399 N  N    . GLY   B 1 162 ? -32.877 25.375 -3.632  1.00 44.47 ? 193 GLY   B N    1 
ATOM   3400 C  CA   . GLY   B 1 162 ? -32.764 24.049 -3.063  1.00 45.02 ? 193 GLY   B CA   1 
ATOM   3401 C  C    . GLY   B 1 162 ? -31.355 23.598 -2.765  1.00 47.05 ? 193 GLY   B C    1 
ATOM   3402 O  O    . GLY   B 1 162 ? -31.165 22.451 -2.340  1.00 43.57 ? 193 GLY   B O    1 
ATOM   3403 N  N    . LYS   B 1 163 ? -30.362 24.446 -2.981  1.00 47.18 ? 194 LYS   B N    1 
ATOM   3404 C  CA   . LYS   B 1 163 ? -28.984 24.062 -2.737  1.00 46.77 ? 194 LYS   B CA   1 
ATOM   3405 C  C    . LYS   B 1 163 ? -28.569 24.473 -1.333  1.00 46.22 ? 194 LYS   B C    1 
ATOM   3406 O  O    . LYS   B 1 163 ? -29.174 25.356 -0.714  1.00 43.77 ? 194 LYS   B O    1 
ATOM   3407 C  CB   . LYS   B 1 163 ? -28.062 24.698 -3.783  1.00 48.21 ? 194 LYS   B CB   1 
ATOM   3408 C  CG   . LYS   B 1 163 ? -28.445 24.345 -5.222  1.00 48.67 ? 194 LYS   B CG   1 
ATOM   3409 C  CD   . LYS   B 1 163 ? -28.601 22.846 -5.356  1.00 50.04 ? 194 LYS   B CD   1 
ATOM   3410 C  CE   . LYS   B 1 163 ? -28.774 22.408 -6.789  1.00 56.34 ? 194 LYS   B CE   1 
ATOM   3411 N  NZ   . LYS   B 1 163 ? -28.722 20.915 -6.846  1.00 61.03 ? 194 LYS   B NZ   1 
ATOM   3412 N  N    . ASN   B 1 164 ? -27.523 23.808 -0.831  1.00 47.19 ? 195 ASN   B N    1 
ATOM   3413 C  CA   . ASN   B 1 164 ? -26.966 24.099 0.479   1.00 46.00 ? 195 ASN   B CA   1 
ATOM   3414 C  C    . ASN   B 1 164 ? -25.904 25.182 0.357   1.00 48.45 ? 195 ASN   B C    1 
ATOM   3415 O  O    . ASN   B 1 164 ? -24.969 25.053 -0.441  1.00 46.09 ? 195 ASN   B O    1 
ATOM   3416 C  CB   . ASN   B 1 164 ? -26.345 22.852 1.110   1.00 48.80 ? 195 ASN   B CB   1 
ATOM   3417 C  CG   . ASN   B 1 164 ? -27.344 21.735 1.312   1.00 52.28 ? 195 ASN   B CG   1 
ATOM   3418 O  OD1  . ASN   B 1 164 ? -28.546 21.968 1.471   1.00 49.36 ? 195 ASN   B OD1  1 
ATOM   3419 N  ND2  . ASN   B 1 164 ? -26.848 20.504 1.303   1.00 52.62 ? 195 ASN   B ND2  1 
ATOM   3420 N  N    . VAL   B 1 165 ? -26.032 26.224 1.178   1.00 45.54 ? 196 VAL   B N    1 
ATOM   3421 C  CA   . VAL   B 1 165 ? -25.115 27.357 1.208   1.00 39.34 ? 196 VAL   B CA   1 
ATOM   3422 C  C    . VAL   B 1 165 ? -24.665 27.564 2.642   1.00 43.22 ? 196 VAL   B C    1 
ATOM   3423 O  O    . VAL   B 1 165 ? -25.502 27.629 3.546   1.00 42.09 ? 196 VAL   B O    1 
ATOM   3424 C  CB   . VAL   B 1 165 ? -25.784 28.642 0.673   1.00 43.08 ? 196 VAL   B CB   1 
ATOM   3425 C  CG1  . VAL   B 1 165 ? -24.844 29.850 0.801   1.00 42.75 ? 196 VAL   B CG1  1 
ATOM   3426 C  CG2  . VAL   B 1 165 ? -26.252 28.457 -0.771  1.00 40.52 ? 196 VAL   B CG2  1 
ATOM   3427 N  N    . VAL   B 1 166 ? -23.356 27.684 2.852   1.00 39.40 ? 197 VAL   B N    1 
ATOM   3428 C  CA   . VAL   B 1 166 ? -22.798 28.073 4.142   1.00 39.53 ? 197 VAL   B CA   1 
ATOM   3429 C  C    . VAL   B 1 166 ? -22.205 29.466 4.009   1.00 43.36 ? 197 VAL   B C    1 
ATOM   3430 O  O    . VAL   B 1 166 ? -21.417 29.729 3.091   1.00 44.61 ? 197 VAL   B O    1 
ATOM   3431 C  CB   . VAL   B 1 166 ? -21.726 27.085 4.631   1.00 40.48 ? 197 VAL   B CB   1 
ATOM   3432 C  CG1  . VAL   B 1 166 ? -21.044 27.618 5.893   1.00 44.10 ? 197 VAL   B CG1  1 
ATOM   3433 C  CG2  . VAL   B 1 166 ? -22.340 25.717 4.881   1.00 44.66 ? 197 VAL   B CG2  1 
ATOM   3434 N  N    . VAL   B 1 167 ? -22.579 30.357 4.917   1.00 41.96 ? 198 VAL   B N    1 
ATOM   3435 C  CA   . VAL   B 1 167 ? -21.950 31.666 5.034   1.00 41.78 ? 198 VAL   B CA   1 
ATOM   3436 C  C    . VAL   B 1 167 ? -21.132 31.674 6.315   1.00 44.06 ? 198 VAL   B C    1 
ATOM   3437 O  O    . VAL   B 1 167 ? -21.635 31.311 7.391   1.00 40.01 ? 198 VAL   B O    1 
ATOM   3438 C  CB   . VAL   B 1 167 ? -22.983 32.804 5.030   1.00 41.80 ? 198 VAL   B CB   1 
ATOM   3439 C  CG1  . VAL   B 1 167 ? -22.284 34.170 5.126   1.00 39.50 ? 198 VAL   B CG1  1 
ATOM   3440 C  CG2  . VAL   B 1 167 ? -23.853 32.719 3.797   1.00 35.57 ? 198 VAL   B CG2  1 
ATOM   3441 N  N    . ALA   B 1 168 ? -19.867 32.062 6.193   1.00 41.40 ? 199 ALA   B N    1 
ATOM   3442 C  CA   . ALA   B 1 168 ? -18.966 32.211 7.327   1.00 41.90 ? 199 ALA   B CA   1 
ATOM   3443 C  C    . ALA   B 1 168 ? -18.886 33.698 7.643   1.00 42.96 ? 199 ALA   B C    1 
ATOM   3444 O  O    . ALA   B 1 168 ? -18.200 34.457 6.951   1.00 40.66 ? 199 ALA   B O    1 
ATOM   3445 C  CB   . ALA   B 1 168 ? -17.591 31.623 7.020   1.00 42.67 ? 199 ALA   B CB   1 
ATOM   3446 N  N    . GLY   B 1 169 ? -19.591 34.110 8.690   1.00 41.58 ? 200 GLY   B N    1 
ATOM   3447 C  CA   . GLY   B 1 169 ? -19.640 35.505 9.096   1.00 38.71 ? 200 GLY   B CA   1 
ATOM   3448 C  C    . GLY   B 1 169 ? -21.087 35.942 9.195   1.00 39.73 ? 200 GLY   B C    1 
ATOM   3449 O  O    . GLY   B 1 169 ? -21.953 35.488 8.442   1.00 39.20 ? 200 GLY   B O    1 
ATOM   3450 N  N    . ARG   B 1 170 ? -21.354 36.855 10.135  1.00 34.59 ? 201 ARG   B N    1 
ATOM   3451 C  CA   . ARG   B 1 170 ? -22.714 37.326 10.376  1.00 37.08 ? 201 ARG   B CA   1 
ATOM   3452 C  C    . ARG   B 1 170 ? -22.774 38.843 10.497  1.00 37.69 ? 201 ARG   B C    1 
ATOM   3453 O  O    . ARG   B 1 170 ? -23.716 39.376 11.106  1.00 35.34 ? 201 ARG   B O    1 
ATOM   3454 C  CB   . ARG   B 1 170 ? -23.290 36.676 11.645  1.00 33.63 ? 201 ARG   B CB   1 
ATOM   3455 C  CG   . ARG   B 1 170 ? -22.443 36.944 12.867  1.00 33.33 ? 201 ARG   B CG   1 
ATOM   3456 C  CD   . ARG   B 1 170 ? -23.048 36.438 14.200  1.00 36.90 ? 201 ARG   B CD   1 
ATOM   3457 N  NE   . ARG   B 1 170 ? -22.079 36.631 15.268  1.00 34.61 ? 201 ARG   B NE   1 
ATOM   3458 C  CZ   . ARG   B 1 170 ? -22.193 36.164 16.506  1.00 41.93 ? 201 ARG   B CZ   1 
ATOM   3459 N  NH1  . ARG   B 1 170 ? -23.253 35.470 16.894  1.00 37.52 ? 201 ARG   B NH1  1 
ATOM   3460 N  NH2  . ARG   B 1 170 ? -21.212 36.388 17.375  1.00 41.53 ? 201 ARG   B NH2  1 
ATOM   3461 N  N    . SER   B 1 171 ? -21.785 39.561 9.964   1.00 35.45 ? 202 SER   B N    1 
ATOM   3462 C  CA   . SER   B 1 171 ? -21.785 41.005 10.157  1.00 36.93 ? 202 SER   B CA   1 
ATOM   3463 C  C    . SER   B 1 171 ? -23.010 41.621 9.491   1.00 35.44 ? 202 SER   B C    1 
ATOM   3464 O  O    . SER   B 1 171 ? -23.545 41.095 8.513   1.00 35.39 ? 202 SER   B O    1 
ATOM   3465 C  CB   . SER   B 1 171 ? -20.505 41.629 9.608   1.00 39.58 ? 202 SER   B CB   1 
ATOM   3466 O  OG   . SER   B 1 171 ? -20.457 41.513 8.195   1.00 39.07 ? 202 SER   B OG   1 
ATOM   3467 N  N    . LYS   B 1 172 ? -23.468 42.742 10.048  1.00 34.25 ? 203 LYS   B N    1 
ATOM   3468 C  CA   . LYS   B 1 172 ? -24.721 43.323 9.587   1.00 33.99 ? 203 LYS   B CA   1 
ATOM   3469 C  C    . LYS   B 1 172 ? -24.607 43.902 8.179   1.00 37.50 ? 203 LYS   B C    1 
ATOM   3470 O  O    . LYS   B 1 172 ? -25.609 43.970 7.467   1.00 35.24 ? 203 LYS   B O    1 
ATOM   3471 C  CB   . LYS   B 1 172 ? -25.191 44.385 10.578  1.00 34.26 ? 203 LYS   B CB   1 
ATOM   3472 C  CG   . LYS   B 1 172 ? -25.459 43.805 11.954  1.00 32.12 ? 203 LYS   B CG   1 
ATOM   3473 C  CD   . LYS   B 1 172 ? -26.357 42.568 11.864  1.00 31.23 ? 203 LYS   B CD   1 
ATOM   3474 C  CE   . LYS   B 1 172 ? -26.773 42.101 13.278  1.00 37.03 ? 203 LYS   B CE   1 
ATOM   3475 N  NZ   . LYS   B 1 172 ? -27.815 41.027 13.231  1.00 35.19 ? 203 LYS   B NZ   1 
ATOM   3476 N  N    . ASN   B 1 173 ? -23.411 44.316 7.756   1.00 36.19 ? 204 ASN   B N    1 
ATOM   3477 C  CA   . ASN   B 1 173 ? -23.249 44.917 6.433   1.00 38.02 ? 204 ASN   B CA   1 
ATOM   3478 C  C    . ASN   B 1 173 ? -22.850 43.912 5.358   1.00 36.41 ? 204 ASN   B C    1 
ATOM   3479 O  O    . ASN   B 1 173 ? -22.996 44.212 4.167   1.00 35.34 ? 204 ASN   B O    1 
ATOM   3480 C  CB   . ASN   B 1 173 ? -22.198 46.040 6.474   1.00 38.20 ? 204 ASN   B CB   1 
ATOM   3481 C  CG   . ASN   B 1 173 ? -22.575 47.201 7.423   1.00 45.29 ? 204 ASN   B CG   1 
ATOM   3482 O  OD1  . ASN   B 1 173 ? -23.750 47.581 7.555   1.00 43.63 ? 204 ASN   B OD1  1 
ATOM   3483 N  ND2  . ASN   B 1 173 ? -21.559 47.786 8.065   1.00 43.68 ? 204 ASN   B ND2  1 
ATOM   3484 N  N    . VAL   B 1 174 ? -22.308 42.750 5.733   1.00 36.62 ? 205 VAL   B N    1 
ATOM   3485 C  CA   . VAL   B 1 174 ? -21.872 41.784 4.729   1.00 39.43 ? 205 VAL   B CA   1 
ATOM   3486 C  C    . VAL   B 1 174 ? -22.496 40.408 4.943   1.00 36.96 ? 205 VAL   B C    1 
ATOM   3487 O  O    . VAL   B 1 174 ? -23.319 39.956 4.137   1.00 35.16 ? 205 VAL   B O    1 
ATOM   3488 C  CB   . VAL   B 1 174 ? -20.333 41.667 4.718   1.00 41.70 ? 205 VAL   B CB   1 
ATOM   3489 C  CG1  . VAL   B 1 174 ? -19.883 40.749 3.583   1.00 35.39 ? 205 VAL   B CG1  1 
ATOM   3490 C  CG2  . VAL   B 1 174 ? -19.678 43.045 4.592   1.00 39.78 ? 205 VAL   B CG2  1 
ATOM   3491 N  N    . GLY   B 1 175 ? -22.127 39.745 6.043   1.00 37.20 ? 206 GLY   B N    1 
ATOM   3492 C  CA   . GLY   B 1 175 ? -22.497 38.344 6.203   1.00 38.07 ? 206 GLY   B CA   1 
ATOM   3493 C  C    . GLY   B 1 175 ? -23.996 38.123 6.311   1.00 36.02 ? 206 GLY   B C    1 
ATOM   3494 O  O    . GLY   B 1 175 ? -24.551 37.233 5.664   1.00 33.82 ? 206 GLY   B O    1 
ATOM   3495 N  N    . MET   B 1 176 ? -24.670 38.920 7.151   1.00 37.39 ? 207 MET   B N    1 
ATOM   3496 C  CA   . MET   B 1 176 ? -26.115 38.762 7.326   1.00 35.50 ? 207 MET   B CA   1 
ATOM   3497 C  C    . MET   B 1 176 ? -26.904 39.051 6.050   1.00 36.96 ? 207 MET   B C    1 
ATOM   3498 O  O    . MET   B 1 176 ? -27.789 38.245 5.705   1.00 33.59 ? 207 MET   B O    1 
ATOM   3499 C  CB   . MET   B 1 176 ? -26.590 39.634 8.501   1.00 35.05 ? 207 MET   B CB   1 
ATOM   3500 C  CG   . MET   B 1 176 ? -28.097 39.570 8.779   1.00 35.23 ? 207 MET   B CG   1 
ATOM   3501 S  SD   . MET   B 1 176 ? -29.115 40.665 7.764   1.00 36.11 ? 207 MET   B SD   1 
ATOM   3502 C  CE   . MET   B 1 176 ? -28.903 42.208 8.662   1.00 34.86 ? 207 MET   B CE   1 
ATOM   3503 N  N    . PRO   B 1 177 ? -26.686 40.165 5.332   1.00 36.41 ? 208 PRO   B N    1 
ATOM   3504 C  CA   . PRO   B 1 177 ? -27.435 40.369 4.071   1.00 34.10 ? 208 PRO   B CA   1 
ATOM   3505 C  C    . PRO   B 1 177 ? -27.176 39.295 3.030   1.00 33.11 ? 208 PRO   B C    1 
ATOM   3506 O  O    . PRO   B 1 177 ? -28.072 38.989 2.234   1.00 33.77 ? 208 PRO   B O    1 
ATOM   3507 C  CB   . PRO   B 1 177 ? -26.971 41.748 3.573   1.00 32.86 ? 208 PRO   B CB   1 
ATOM   3508 C  CG   . PRO   B 1 177 ? -26.250 42.388 4.708   1.00 36.45 ? 208 PRO   B CG   1 
ATOM   3509 C  CD   . PRO   B 1 177 ? -25.821 41.311 5.666   1.00 36.06 ? 208 PRO   B CD   1 
ATOM   3510 N  N    . ILE   B 1 178 ? -25.975 38.716 2.994   1.00 38.34 ? 209 ILE   B N    1 
ATOM   3511 C  CA   . ILE   B 1 178 ? -25.721 37.613 2.068   1.00 35.06 ? 209 ILE   B CA   1 
ATOM   3512 C  C    . ILE   B 1 178 ? -26.635 36.434 2.392   1.00 37.05 ? 209 ILE   B C    1 
ATOM   3513 O  O    . ILE   B 1 178 ? -27.309 35.881 1.512   1.00 35.04 ? 209 ILE   B O    1 
ATOM   3514 C  CB   . ILE   B 1 178 ? -24.242 37.198 2.131   1.00 38.28 ? 209 ILE   B CB   1 
ATOM   3515 C  CG1  . ILE   B 1 178 ? -23.354 38.251 1.459   1.00 37.97 ? 209 ILE   B CG1  1 
ATOM   3516 C  CG2  . ILE   B 1 178 ? -24.056 35.799 1.520   1.00 32.08 ? 209 ILE   B CG2  1 
ATOM   3517 C  CD1  . ILE   B 1 178 ? -21.897 38.091 1.815   1.00 38.94 ? 209 ILE   B CD1  1 
ATOM   3518 N  N    . ALA   B 1 179 ? -26.681 36.044 3.673   1.00 33.61 ? 210 ALA   B N    1 
ATOM   3519 C  CA   . ALA   B 1 179 ? -27.558 34.948 4.086   1.00 36.47 ? 210 ALA   B CA   1 
ATOM   3520 C  C    . ALA   B 1 179 ? -29.018 35.274 3.799   1.00 34.75 ? 210 ALA   B C    1 
ATOM   3521 O  O    . ALA   B 1 179 ? -29.776 34.413 3.336   1.00 35.17 ? 210 ALA   B O    1 
ATOM   3522 C  CB   . ALA   B 1 179 ? -27.350 34.643 5.568   1.00 32.36 ? 210 ALA   B CB   1 
ATOM   3523 N  N    . MET   B 1 180 ? -29.419 36.529 4.023   1.00 34.23 ? 211 MET   B N    1 
ATOM   3524 C  CA   . MET   B 1 180 ? -30.784 36.949 3.713   1.00 33.56 ? 211 MET   B CA   1 
ATOM   3525 C  C    . MET   B 1 180 ? -31.091 36.791 2.224   1.00 38.42 ? 211 MET   B C    1 
ATOM   3526 O  O    . MET   B 1 180 ? -32.094 36.181 1.846   1.00 37.01 ? 211 MET   B O    1 
ATOM   3527 C  CB   . MET   B 1 180 ? -30.987 38.402 4.148   1.00 32.12 ? 211 MET   B CB   1 
ATOM   3528 C  CG   . MET   B 1 180 ? -32.412 38.915 3.992   1.00 36.12 ? 211 MET   B CG   1 
ATOM   3529 S  SD   . MET   B 1 180 ? -33.618 38.025 5.039   1.00 38.42 ? 211 MET   B SD   1 
ATOM   3530 C  CE   . MET   B 1 180 ? -32.775 38.034 6.600   1.00 33.66 ? 211 MET   B CE   1 
ATOM   3531 N  N    . LEU   B 1 181 ? -30.243 37.314 1.354   1.00 35.59 ? 212 LEU   B N    1 
ATOM   3532 C  CA   . LEU   B 1 181 ? -30.541 37.263 -0.097  1.00 38.98 ? 212 LEU   B CA   1 
ATOM   3533 C  C    . LEU   B 1 181 ? -30.587 35.814 -0.581  1.00 33.24 ? 212 LEU   B C    1 
ATOM   3534 O  O    . LEU   B 1 181 ? -31.467 35.490 -1.364  1.00 39.60 ? 212 LEU   B O    1 
ATOM   3535 C  CB   . LEU   B 1 181 ? -29.447 38.030 -0.844  1.00 37.12 ? 212 LEU   B CB   1 
ATOM   3536 C  CG   . LEU   B 1 181 ? -29.447 39.546 -0.682  1.00 38.82 ? 212 LEU   B CG   1 
ATOM   3537 C  CD1  . LEU   B 1 181 ? -28.178 40.140 -1.271  1.00 40.11 ? 212 LEU   B CD1  1 
ATOM   3538 C  CD2  . LEU   B 1 181 ? -30.673 40.158 -1.335  1.00 36.14 ? 212 LEU   B CD2  1 
ATOM   3539 N  N    . LEU   B 1 182 ? -29.695 34.966 -0.091  1.00 39.71 ? 213 LEU   B N    1 
ATOM   3540 C  CA   . LEU   B 1 182 ? -29.585 33.591 -0.645  1.00 40.48 ? 213 LEU   B CA   1 
ATOM   3541 C  C    . LEU   B 1 182 ? -30.720 32.665 -0.196  1.00 42.34 ? 213 LEU   B C    1 
ATOM   3542 O  O    . LEU   B 1 182 ? -31.092 31.804 -0.996  1.00 40.61 ? 213 LEU   B O    1 
ATOM   3543 C  CB   . LEU   B 1 182 ? -28.223 33.027 -0.239  1.00 39.29 ? 213 LEU   B CB   1 
ATOM   3544 C  CG   . LEU   B 1 182 ? -27.117 33.153 -1.282  1.00 45.50 ? 213 LEU   B CG   1 
ATOM   3545 C  CD1  . LEU   B 1 182 ? -27.613 32.707 -2.647  1.00 43.83 ? 213 LEU   B CD1  1 
ATOM   3546 C  CD2  . LEU   B 1 182 ? -26.596 34.575 -1.340  1.00 44.36 ? 213 LEU   B CD2  1 
ATOM   3547 N  N    . HIS   B 1 183 ? -31.253 32.823 1.016   1.00 34.56 ? 214 HIS   B N    1 
ATOM   3548 C  CA   . HIS   B 1 183 ? -32.253 31.860 1.474   1.00 33.87 ? 214 HIS   B CA   1 
ATOM   3549 C  C    . HIS   B 1 183 ? -33.690 32.259 1.147   1.00 34.83 ? 214 HIS   B C    1 
ATOM   3550 O  O    . HIS   B 1 183 ? -34.597 31.428 1.287   1.00 35.88 ? 214 HIS   B O    1 
ATOM   3551 C  CB   . HIS   B 1 183 ? -32.125 31.616 2.990   1.00 34.34 ? 214 HIS   B CB   1 
ATOM   3552 C  CG   . HIS   B 1 183 ? -32.887 32.594 3.853   1.00 36.82 ? 214 HIS   B CG   1 
ATOM   3553 N  ND1  . HIS   B 1 183 ? -32.279 33.664 4.483   1.00 37.72 ? 214 HIS   B ND1  1 
ATOM   3554 C  CD2  . HIS   B 1 183 ? -34.187 32.620 4.249   1.00 38.33 ? 214 HIS   B CD2  1 
ATOM   3555 C  CE1  . HIS   B 1 183 ? -33.174 34.325 5.200   1.00 34.66 ? 214 HIS   B CE1  1 
ATOM   3556 N  NE2  . HIS   B 1 183 ? -34.337 33.710 5.079   1.00 32.95 ? 214 HIS   B NE2  1 
ATOM   3557 N  N    . THR   B 1 184 ? -33.931 33.486 0.684   1.00 34.72 ? 215 THR   B N    1 
ATOM   3558 C  CA   . THR   B 1 184 ? -35.300 33.979 0.640   1.00 33.17 ? 215 THR   B CA   1 
ATOM   3559 C  C    . THR   B 1 184 ? -35.992 33.664 -0.687  1.00 38.08 ? 215 THR   B C    1 
ATOM   3560 O  O    . THR   B 1 184 ? -35.395 33.128 -1.628  1.00 37.88 ? 215 THR   B O    1 
ATOM   3561 C  CB   . THR   B 1 184 ? -35.312 35.471 0.938   1.00 37.21 ? 215 THR   B CB   1 
ATOM   3562 O  OG1  . THR   B 1 184 ? -34.296 36.127 0.159   1.00 36.02 ? 215 THR   B OG1  1 
ATOM   3563 C  CG2  . THR   B 1 184 ? -35.083 35.704 2.478   1.00 32.57 ? 215 THR   B CG2  1 
ATOM   3564 N  N    . ASP   B 1 185 ? -37.277 34.013 -0.748  1.00 36.73 ? 216 ASP   B N    1 
ATOM   3565 C  CA   . ASP   B 1 185 ? -38.195 33.472 -1.747  1.00 39.54 ? 216 ASP   B CA   1 
ATOM   3566 C  C    . ASP   B 1 185 ? -37.971 34.149 -3.094  1.00 38.11 ? 216 ASP   B C    1 
ATOM   3567 O  O    . ASP   B 1 185 ? -38.004 35.379 -3.185  1.00 37.23 ? 216 ASP   B O    1 
ATOM   3568 C  CB   . ASP   B 1 185 ? -39.643 33.674 -1.285  1.00 35.09 ? 216 ASP   B CB   1 
ATOM   3569 C  CG   . ASP   B 1 185 ? -40.656 32.807 -2.052  1.00 42.80 ? 216 ASP   B CG   1 
ATOM   3570 O  OD1  . ASP   B 1 185 ? -40.554 32.661 -3.296  1.00 38.71 ? 216 ASP   B OD1  1 
ATOM   3571 O  OD2  . ASP   B 1 185 ? -41.590 32.292 -1.401  1.00 41.40 ? 216 ASP   B OD2  1 
ATOM   3572 N  N    . GLY   B 1 186 ? -37.780 33.340 -4.144  1.00 42.46 ? 217 GLY   B N    1 
ATOM   3573 C  CA   . GLY   B 1 186 ? -37.595 33.880 -5.483  1.00 39.96 ? 217 GLY   B CA   1 
ATOM   3574 C  C    . GLY   B 1 186 ? -38.784 34.673 -5.969  1.00 41.21 ? 217 GLY   B C    1 
ATOM   3575 O  O    . GLY   B 1 186 ? -38.641 35.505 -6.863  1.00 44.09 ? 217 GLY   B O    1 
ATOM   3576 N  N    . ALA   B 1 187 ? -39.952 34.460 -5.376  1.00 42.49 ? 218 ALA   B N    1 
ATOM   3577 C  CA   . ALA   B 1 187 ? -41.180 35.080 -5.840  1.00 38.55 ? 218 ALA   B CA   1 
ATOM   3578 C  C    . ALA   B 1 187 ? -41.558 36.350 -5.087  1.00 39.96 ? 218 ALA   B C    1 
ATOM   3579 O  O    . ALA   B 1 187 ? -42.600 36.937 -5.396  1.00 41.72 ? 218 ALA   B O    1 
ATOM   3580 C  CB   . ALA   B 1 187 ? -42.329 34.062 -5.758  1.00 42.19 ? 218 ALA   B CB   1 
ATOM   3581 N  N    . HIS   B 1 188 ? -40.758 36.790 -4.108  1.00 41.80 ? 219 HIS   B N    1 
ATOM   3582 C  CA   . HIS   B 1 188 ? -41.077 37.998 -3.350  1.00 41.60 ? 219 HIS   B CA   1 
ATOM   3583 C  C    . HIS   B 1 188 ? -40.658 39.244 -4.124  1.00 40.93 ? 219 HIS   B C    1 
ATOM   3584 O  O    . HIS   B 1 188 ? -39.913 39.161 -5.100  1.00 38.78 ? 219 HIS   B O    1 
ATOM   3585 C  CB   . HIS   B 1 188 ? -40.392 37.979 -1.974  1.00 43.87 ? 219 HIS   B CB   1 
ATOM   3586 C  CG   . HIS   B 1 188 ? -41.017 37.027 -1.005  1.00 42.03 ? 219 HIS   B CG   1 
ATOM   3587 N  ND1  . HIS   B 1 188 ? -40.478 36.761 0.238   1.00 43.46 ? 219 HIS   B ND1  1 
ATOM   3588 C  CD2  . HIS   B 1 188 ? -42.135 36.268 -1.103  1.00 42.34 ? 219 HIS   B CD2  1 
ATOM   3589 C  CE1  . HIS   B 1 188 ? -41.245 35.886 0.866   1.00 42.32 ? 219 HIS   B CE1  1 
ATOM   3590 N  NE2  . HIS   B 1 188 ? -42.258 35.575 0.076   1.00 46.89 ? 219 HIS   B NE2  1 
ATOM   3591 N  N    . GLU   B 1 189 ? -41.130 40.414 -3.660  1.00 36.56 ? 220 GLU   B N    1 
ATOM   3592 C  CA   . GLU   B 1 189 ? -40.844 41.698 -4.307  1.00 45.38 ? 220 GLU   B CA   1 
ATOM   3593 C  C    . GLU   B 1 189 ? -39.389 41.818 -4.741  1.00 46.87 ? 220 GLU   B C    1 
ATOM   3594 O  O    . GLU   B 1 189 ? -39.086 42.073 -5.914  1.00 48.12 ? 220 GLU   B O    1 
ATOM   3595 C  CB   . GLU   B 1 189 ? -41.177 42.859 -3.370  1.00 44.25 ? 220 GLU   B CB   1 
ATOM   3596 C  CG   . GLU   B 1 189 ? -42.564 43.436 -3.529  1.00 51.79 ? 220 GLU   B CG   1 
ATOM   3597 C  CD   . GLU   B 1 189 ? -42.802 44.640 -2.624  1.00 50.31 ? 220 GLU   B CD   1 
ATOM   3598 O  OE1  . GLU   B 1 189 ? -41.818 45.235 -2.129  1.00 49.40 ? 220 GLU   B OE1  1 
ATOM   3599 O  OE2  . GLU   B 1 189 ? -43.977 45.005 -2.418  1.00 57.25 ? 220 GLU   B OE2  1 
ATOM   3600 N  N    . ARG   B 1 190 ? -38.480 41.658 -3.791  1.00 39.20 ? 221 ARG   B N    1 
ATOM   3601 C  CA   . ARG   B 1 190 ? -37.072 41.490 -4.098  1.00 39.82 ? 221 ARG   B CA   1 
ATOM   3602 C  C    . ARG   B 1 190 ? -36.780 39.998 -4.053  1.00 41.06 ? 221 ARG   B C    1 
ATOM   3603 O  O    . ARG   B 1 190 ? -36.847 39.397 -2.968  1.00 39.05 ? 221 ARG   B O    1 
ATOM   3604 C  CB   . ARG   B 1 190 ? -36.205 42.254 -3.095  1.00 40.59 ? 221 ARG   B CB   1 
ATOM   3605 C  CG   . ARG   B 1 190 ? -34.729 42.353 -3.413  1.00 39.22 ? 221 ARG   B CG   1 
ATOM   3606 C  CD   . ARG   B 1 190 ? -33.951 41.196 -2.808  1.00 40.17 ? 221 ARG   B CD   1 
ATOM   3607 N  NE   . ARG   B 1 190 ? -34.085 41.134 -1.357  1.00 40.81 ? 221 ARG   B NE   1 
ATOM   3608 C  CZ   . ARG   B 1 190 ? -34.240 40.015 -0.660  1.00 37.42 ? 221 ARG   B CZ   1 
ATOM   3609 N  NH1  . ARG   B 1 190 ? -34.408 40.038 0.653   1.00 38.49 ? 221 ARG   B NH1  1 
ATOM   3610 N  NH2  . ARG   B 1 190 ? -34.254 38.847 -1.296  1.00 36.50 ? 221 ARG   B NH2  1 
ATOM   3611 N  N    . PRO   B 1 191 ? -36.489 39.356 -5.184  1.00 37.73 ? 222 PRO   B N    1 
ATOM   3612 C  CA   . PRO   B 1 191 ? -36.281 37.904 -5.178  1.00 37.95 ? 222 PRO   B CA   1 
ATOM   3613 C  C    . PRO   B 1 191 ? -35.061 37.502 -4.372  1.00 38.85 ? 222 PRO   B C    1 
ATOM   3614 O  O    . PRO   B 1 191 ? -34.076 38.241 -4.279  1.00 38.41 ? 222 PRO   B O    1 
ATOM   3615 C  CB   . PRO   B 1 191 ? -36.086 37.559 -6.666  1.00 35.23 ? 222 PRO   B CB   1 
ATOM   3616 C  CG   . PRO   B 1 191 ? -36.729 38.687 -7.409  1.00 35.15 ? 222 PRO   B CG   1 
ATOM   3617 C  CD   . PRO   B 1 191 ? -36.559 39.909 -6.552  1.00 42.07 ? 222 PRO   B CD   1 
ATOM   3618 N  N    . GLY   B 1 192 ? -35.129 36.296 -3.807  1.00 37.26 ? 223 GLY   B N    1 
ATOM   3619 C  CA   . GLY   B 1 192 ? -34.000 35.671 -3.160  1.00 36.69 ? 223 GLY   B CA   1 
ATOM   3620 C  C    . GLY   B 1 192 ? -33.607 34.391 -3.879  1.00 38.64 ? 223 GLY   B C    1 
ATOM   3621 O  O    . GLY   B 1 192 ? -34.241 33.980 -4.848  1.00 36.68 ? 223 GLY   B O    1 
ATOM   3622 N  N    . GLY   B 1 193 ? -32.565 33.750 -3.353  1.00 40.64 ? 224 GLY   B N    1 
ATOM   3623 C  CA   . GLY   B 1 193 ? -31.986 32.565 -3.957  1.00 39.84 ? 224 GLY   B CA   1 
ATOM   3624 C  C    . GLY   B 1 193 ? -32.632 31.228 -3.623  1.00 41.75 ? 224 GLY   B C    1 
ATOM   3625 O  O    . GLY   B 1 193 ? -32.277 30.232 -4.260  1.00 42.12 ? 224 GLY   B O    1 
ATOM   3626 N  N    . ASP   B 1 194 ? -33.545 31.162 -2.645  1.00 40.95 ? 225 ASP   B N    1 
ATOM   3627 C  CA   . ASP   B 1 194 ? -34.229 29.910 -2.281  1.00 37.93 ? 225 ASP   B CA   1 
ATOM   3628 C  C    . ASP   B 1 194 ? -33.253 28.795 -1.902  1.00 38.33 ? 225 ASP   B C    1 
ATOM   3629 O  O    . ASP   B 1 194 ? -33.545 27.612 -2.093  1.00 39.96 ? 225 ASP   B O    1 
ATOM   3630 C  CB   . ASP   B 1 194 ? -35.153 29.425 -3.409  1.00 40.87 ? 225 ASP   B CB   1 
ATOM   3631 C  CG   . ASP   B 1 194 ? -36.436 30.227 -3.510  1.00 42.53 ? 225 ASP   B CG   1 
ATOM   3632 O  OD1  . ASP   B 1 194 ? -37.138 30.374 -2.474  1.00 36.87 ? 225 ASP   B OD1  1 
ATOM   3633 O  OD2  . ASP   B 1 194 ? -36.750 30.708 -4.633  1.00 41.23 ? 225 ASP   B OD2  1 
ATOM   3634 N  N    . ALA   B 1 195 ? -32.089 29.145 -1.370  1.00 35.67 ? 226 ALA   B N    1 
ATOM   3635 C  CA   . ALA   B 1 195 ? -31.149 28.154 -0.871  1.00 37.84 ? 226 ALA   B CA   1 
ATOM   3636 C  C    . ALA   B 1 195 ? -31.442 27.780 0.582   1.00 41.95 ? 226 ALA   B C    1 
ATOM   3637 O  O    . ALA   B 1 195 ? -32.158 28.473 1.305   1.00 40.50 ? 226 ALA   B O    1 
ATOM   3638 C  CB   . ALA   B 1 195 ? -29.719 28.674 -0.959  1.00 37.75 ? 226 ALA   B CB   1 
ATOM   3639 N  N    . THR   B 1 196 ? -30.831 26.676 1.008   1.00 41.87 ? 227 THR   B N    1 
ATOM   3640 C  CA   . THR   B 1 196 ? -30.768 26.282 2.407   1.00 43.29 ? 227 THR   B CA   1 
ATOM   3641 C  C    . THR   B 1 196 ? -29.477 26.845 2.986   1.00 41.75 ? 227 THR   B C    1 
ATOM   3642 O  O    . THR   B 1 196 ? -28.386 26.352 2.686   1.00 44.02 ? 227 THR   B O    1 
ATOM   3643 C  CB   . THR   B 1 196 ? -30.814 24.760 2.547   1.00 44.16 ? 227 THR   B CB   1 
ATOM   3644 O  OG1  . THR   B 1 196 ? -31.974 24.253 1.879   1.00 40.87 ? 227 THR   B OG1  1 
ATOM   3645 C  CG2  . THR   B 1 196 ? -30.881 24.367 4.024   1.00 47.17 ? 227 THR   B CG2  1 
ATOM   3646 N  N    . VAL   B 1 197 ? -29.591 27.869 3.824   1.00 39.66 ? 228 VAL   B N    1 
ATOM   3647 C  CA   . VAL   B 1 197 ? -28.436 28.662 4.233   1.00 38.23 ? 228 VAL   B CA   1 
ATOM   3648 C  C    . VAL   B 1 197 ? -28.106 28.365 5.686   1.00 40.06 ? 228 VAL   B C    1 
ATOM   3649 O  O    . VAL   B 1 197 ? -28.971 28.473 6.565   1.00 38.68 ? 228 VAL   B O    1 
ATOM   3650 C  CB   . VAL   B 1 197 ? -28.676 30.167 4.013   1.00 35.92 ? 228 VAL   B CB   1 
ATOM   3651 C  CG1  . VAL   B 1 197 ? -27.568 30.976 4.670   1.00 34.46 ? 228 VAL   B CG1  1 
ATOM   3652 C  CG2  . VAL   B 1 197 ? -28.754 30.485 2.488   1.00 36.79 ? 228 VAL   B CG2  1 
ATOM   3653 N  N    . THR   B 1 198 ? -26.851 28.005 5.934   1.00 37.11 ? 229 THR   B N    1 
ATOM   3654 C  CA   . THR   B 1 198 ? -26.312 27.918 7.281   1.00 39.68 ? 229 THR   B CA   1 
ATOM   3655 C  C    . THR   B 1 198 ? -25.469 29.155 7.565   1.00 42.66 ? 229 THR   B C    1 
ATOM   3656 O  O    . THR   B 1 198 ? -24.588 29.514 6.768   1.00 41.10 ? 229 THR   B O    1 
ATOM   3657 C  CB   . THR   B 1 198 ? -25.472 26.650 7.451   1.00 41.55 ? 229 THR   B CB   1 
ATOM   3658 O  OG1  . THR   B 1 198 ? -26.303 25.500 7.249   1.00 44.47 ? 229 THR   B OG1  1 
ATOM   3659 C  CG2  . THR   B 1 198 ? -24.843 26.598 8.827   1.00 41.55 ? 229 THR   B CG2  1 
ATOM   3660 N  N    . ILE   B 1 199 ? -25.744 29.799 8.696   1.00 41.94 ? 230 ILE   B N    1 
ATOM   3661 C  CA   . ILE   B 1 199 ? -24.980 30.943 9.177   1.00 43.12 ? 230 ILE   B CA   1 
ATOM   3662 C  C    . ILE   B 1 199 ? -24.000 30.449 10.234  1.00 43.64 ? 230 ILE   B C    1 
ATOM   3663 O  O    . ILE   B 1 199 ? -24.412 29.901 11.265  1.00 43.94 ? 230 ILE   B O    1 
ATOM   3664 C  CB   . ILE   B 1 199 ? -25.906 32.025 9.756   1.00 44.70 ? 230 ILE   B CB   1 
ATOM   3665 C  CG1  . ILE   B 1 199 ? -26.903 32.501 8.688   1.00 39.40 ? 230 ILE   B CG1  1 
ATOM   3666 C  CG2  . ILE   B 1 199 ? -25.090 33.173 10.341  1.00 40.45 ? 230 ILE   B CG2  1 
ATOM   3667 C  CD1  . ILE   B 1 199 ? -28.148 33.251 9.278   1.00 40.10 ? 230 ILE   B CD1  1 
ATOM   3668 N  N    . SER   B 1 200 ? -22.707 30.651 9.989   1.00 40.69 ? 231 SER   B N    1 
ATOM   3669 C  CA   . SER   B 1 200 ? -21.665 30.375 10.963  1.00 39.29 ? 231 SER   B CA   1 
ATOM   3670 C  C    . SER   B 1 200 ? -20.941 31.670 11.302  1.00 39.71 ? 231 SER   B C    1 
ATOM   3671 O  O    . SER   B 1 200 ? -21.067 32.675 10.603  1.00 36.74 ? 231 SER   B O    1 
ATOM   3672 C  CB   . SER   B 1 200 ? -20.673 29.334 10.446  1.00 41.34 ? 231 SER   B CB   1 
ATOM   3673 O  OG   . SER   B 1 200 ? -19.913 29.867 9.378   1.00 47.00 ? 231 SER   B OG   1 
ATOM   3674 N  N    . HIS   B 1 201 ? -20.199 31.651 12.401  1.00 38.92 ? 232 HIS   B N    1 
ATOM   3675 C  CA   . HIS   B 1 201 ? -19.623 32.873 12.942  1.00 40.58 ? 232 HIS   B CA   1 
ATOM   3676 C  C    . HIS   B 1 201 ? -18.540 32.500 13.946  1.00 43.24 ? 232 HIS   B C    1 
ATOM   3677 O  O    . HIS   B 1 201 ? -18.156 31.333 14.062  1.00 45.43 ? 232 HIS   B O    1 
ATOM   3678 C  CB   . HIS   B 1 201 ? -20.707 33.739 13.579  1.00 42.03 ? 232 HIS   B CB   1 
ATOM   3679 C  CG   . HIS   B 1 201 ? -21.618 32.972 14.479  1.00 39.89 ? 232 HIS   B CG   1 
ATOM   3680 N  ND1  . HIS   B 1 201 ? -21.217 32.505 15.708  1.00 37.62 ? 232 HIS   B ND1  1 
ATOM   3681 C  CD2  . HIS   B 1 201 ? -22.898 32.560 14.316  1.00 37.46 ? 232 HIS   B CD2  1 
ATOM   3682 C  CE1  . HIS   B 1 201 ? -22.222 31.864 16.279  1.00 40.52 ? 232 HIS   B CE1  1 
ATOM   3683 N  NE2  . HIS   B 1 201 ? -23.250 31.876 15.452  1.00 40.21 ? 232 HIS   B NE2  1 
ATOM   3684 N  N    . ARG   B 1 202 ? -18.078 33.496 14.703  1.00 41.49 ? 233 ARG   B N    1 
ATOM   3685 C  CA   . ARG   B 1 202 ? -16.915 33.321 15.566  1.00 44.37 ? 233 ARG   B CA   1 
ATOM   3686 C  C    . ARG   B 1 202 ? -17.101 32.265 16.658  1.00 47.93 ? 233 ARG   B C    1 
ATOM   3687 O  O    . ARG   B 1 202 ? -16.101 31.805 17.219  1.00 49.71 ? 233 ARG   B O    1 
ATOM   3688 C  CB   . ARG   B 1 202 ? -16.545 34.655 16.212  1.00 44.72 ? 233 ARG   B CB   1 
ATOM   3689 C  CG   . ARG   B 1 202 ? -17.529 35.103 17.291  1.00 42.83 ? 233 ARG   B CG   1 
ATOM   3690 C  CD   . ARG   B 1 202 ? -17.189 36.500 17.822  1.00 44.84 ? 233 ARG   B CD   1 
ATOM   3691 N  NE   . ARG   B 1 202 ? -17.098 37.474 16.740  1.00 48.65 ? 233 ARG   B NE   1 
ATOM   3692 C  CZ   . ARG   B 1 202 ? -15.977 38.052 16.324  1.00 48.27 ? 233 ARG   B CZ   1 
ATOM   3693 N  NH1  . ARG   B 1 202 ? -15.982 38.937 15.340  1.00 46.82 ? 233 ARG   B NH1  1 
ATOM   3694 N  NH2  . ARG   B 1 202 ? -14.826 37.752 16.923  1.00 47.98 ? 233 ARG   B NH2  1 
ATOM   3695 N  N    . TYR   B 1 203 ? -18.333 31.880 17.001  1.00 47.90 ? 234 TYR   B N    1 
ATOM   3696 C  CA   . TYR   B 1 203 ? -18.535 30.828 17.994  1.00 46.12 ? 234 TYR   B CA   1 
ATOM   3697 C  C    . TYR   B 1 203 ? -18.900 29.495 17.360  1.00 47.80 ? 234 TYR   B C    1 
ATOM   3698 O  O    . TYR   B 1 203 ? -19.214 28.543 18.080  1.00 49.17 ? 234 TYR   B O    1 
ATOM   3699 C  CB   . TYR   B 1 203 ? -19.596 31.235 19.024  1.00 41.69 ? 234 TYR   B CB   1 
ATOM   3700 C  CG   . TYR   B 1 203 ? -19.188 32.463 19.804  1.00 46.69 ? 234 TYR   B CG   1 
ATOM   3701 C  CD1  . TYR   B 1 203 ? -18.029 32.465 20.570  1.00 48.96 ? 234 TYR   B CD1  1 
ATOM   3702 C  CD2  . TYR   B 1 203 ? -19.935 33.628 19.748  1.00 43.19 ? 234 TYR   B CD2  1 
ATOM   3703 C  CE1  . TYR   B 1 203 ? -17.634 33.587 21.260  1.00 47.66 ? 234 TYR   B CE1  1 
ATOM   3704 C  CE2  . TYR   B 1 203 ? -19.547 34.759 20.433  1.00 45.65 ? 234 TYR   B CE2  1 
ATOM   3705 C  CZ   . TYR   B 1 203 ? -18.398 34.732 21.190  1.00 49.51 ? 234 TYR   B CZ   1 
ATOM   3706 O  OH   . TYR   B 1 203 ? -18.006 35.852 21.881  1.00 49.36 ? 234 TYR   B OH   1 
ATOM   3707 N  N    . THR   B 1 204 ? -18.861 29.400 16.040  1.00 44.27 ? 235 THR   B N    1 
ATOM   3708 C  CA   . THR   B 1 204 ? -19.067 28.113 15.390  1.00 47.86 ? 235 THR   B CA   1 
ATOM   3709 C  C    . THR   B 1 204 ? -17.770 27.320 15.490  1.00 52.18 ? 235 THR   B C    1 
ATOM   3710 O  O    . THR   B 1 204 ? -16.767 27.713 14.883  1.00 50.74 ? 235 THR   B O    1 
ATOM   3711 C  CB   . THR   B 1 204 ? -19.470 28.296 13.924  1.00 45.29 ? 235 THR   B CB   1 
ATOM   3712 O  OG1  . THR   B 1 204 ? -20.703 29.026 13.845  1.00 44.99 ? 235 THR   B OG1  1 
ATOM   3713 C  CG2  . THR   B 1 204 ? -19.630 26.939 13.228  1.00 48.91 ? 235 THR   B CG2  1 
ATOM   3714 N  N    . PRO   B 1 205 ? -17.737 26.208 16.230  1.00 53.37 ? 236 PRO   B N    1 
ATOM   3715 C  CA   . PRO   B 1 205 ? -16.489 25.445 16.334  1.00 57.39 ? 236 PRO   B CA   1 
ATOM   3716 C  C    . PRO   B 1 205 ? -16.023 24.969 14.966  1.00 53.57 ? 236 PRO   B C    1 
ATOM   3717 O  O    . PRO   B 1 205 ? -16.827 24.674 14.078  1.00 52.79 ? 236 PRO   B O    1 
ATOM   3718 C  CB   . PRO   B 1 205 ? -16.862 24.271 17.250  1.00 56.34 ? 236 PRO   B CB   1 
ATOM   3719 C  CG   . PRO   B 1 205 ? -18.019 24.782 18.049  1.00 53.53 ? 236 PRO   B CG   1 
ATOM   3720 C  CD   . PRO   B 1 205 ? -18.802 25.618 17.058  1.00 50.64 ? 236 PRO   B CD   1 
ATOM   3721 N  N    . LYS   B 1 206 ? -14.698 24.916 14.804  1.00 57.46 ? 237 LYS   B N    1 
ATOM   3722 C  CA   . LYS   B 1 206 ? -14.109 24.565 13.515  1.00 55.96 ? 237 LYS   B CA   1 
ATOM   3723 C  C    . LYS   B 1 206 ? -14.697 23.269 12.966  1.00 58.69 ? 237 LYS   B C    1 
ATOM   3724 O  O    . LYS   B 1 206 ? -15.071 23.198 11.790  1.00 53.81 ? 237 LYS   B O    1 
ATOM   3725 C  CB   . LYS   B 1 206 ? -12.592 24.457 13.662  1.00 60.76 ? 237 LYS   B CB   1 
ATOM   3726 C  CG   . LYS   B 1 206 ? -11.850 24.173 12.372  1.00 67.73 ? 237 LYS   B CG   1 
ATOM   3727 C  CD   . LYS   B 1 206 ? -10.389 23.830 12.647  1.00 74.39 ? 237 LYS   B CD   1 
ATOM   3728 C  CE   . LYS   B 1 206 ? -10.261 23.008 13.921  1.00 72.95 ? 237 LYS   B CE   1 
ATOM   3729 N  NZ   . LYS   B 1 206 ? -8.836  22.940 14.354  1.00 76.38 ? 237 LYS   B NZ   1 
ATOM   3730 N  N    . GLU   B 1 207 ? -14.832 22.247 13.818  1.00 61.41 ? 238 GLU   B N    1 
ATOM   3731 C  CA   . GLU   B 1 207 ? -15.347 20.958 13.357  1.00 62.79 ? 238 GLU   B CA   1 
ATOM   3732 C  C    . GLU   B 1 207 ? -16.793 21.077 12.888  1.00 56.64 ? 238 GLU   B C    1 
ATOM   3733 O  O    . GLU   B 1 207 ? -17.201 20.391 11.946  1.00 57.73 ? 238 GLU   B O    1 
ATOM   3734 C  CB   . GLU   B 1 207 ? -15.239 19.899 14.463  1.00 60.94 ? 238 GLU   B CB   1 
ATOM   3735 C  CG   . GLU   B 1 207 ? -14.055 20.070 15.413  1.00 67.40 ? 238 GLU   B CG   1 
ATOM   3736 C  CD   . GLU   B 1 207 ? -14.290 21.155 16.457  1.00 69.82 ? 238 GLU   B CD   1 
ATOM   3737 O  OE1  . GLU   B 1 207 ? -15.469 21.406 16.797  1.00 71.29 ? 238 GLU   B OE1  1 
ATOM   3738 O  OE2  . GLU   B 1 207 ? -13.300 21.767 16.926  1.00 73.33 ? 238 GLU   B OE2  1 
ATOM   3739 N  N    . GLN   B 1 208 ? -17.594 21.923 13.549  1.00 57.01 ? 239 GLN   B N    1 
ATOM   3740 C  CA   . GLN   B 1 208 ? -18.978 22.101 13.116  1.00 53.78 ? 239 GLN   B CA   1 
ATOM   3741 C  C    . GLN   B 1 208 ? -19.060 22.866 11.805  1.00 51.10 ? 239 GLN   B C    1 
ATOM   3742 O  O    . GLN   B 1 208 ? -19.983 22.636 11.015  1.00 46.96 ? 239 GLN   B O    1 
ATOM   3743 C  CB   . GLN   B 1 208 ? -19.788 22.819 14.196  1.00 56.12 ? 239 GLN   B CB   1 
ATOM   3744 C  CG   . GLN   B 1 208 ? -19.776 22.100 15.544  1.00 57.84 ? 239 GLN   B CG   1 
ATOM   3745 C  CD   . GLN   B 1 208 ? -20.119 20.623 15.414  1.00 59.16 ? 239 GLN   B CD   1 
ATOM   3746 O  OE1  . GLN   B 1 208 ? -21.087 20.247 14.739  1.00 58.32 ? 239 GLN   B OE1  1 
ATOM   3747 N  NE2  . GLN   B 1 208 ? -19.311 19.775 16.044  1.00 61.36 ? 239 GLN   B NE2  1 
ATOM   3748 N  N    . LEU   B 1 209 ? -18.133 23.799 11.571  1.00 48.66 ? 240 LEU   B N    1 
ATOM   3749 C  CA   . LEU   B 1 209 ? -18.088 24.473 10.279  1.00 49.77 ? 240 LEU   B CA   1 
ATOM   3750 C  C    . LEU   B 1 209 ? -17.824 23.468 9.165   1.00 50.72 ? 240 LEU   B C    1 
ATOM   3751 O  O    . LEU   B 1 209 ? -18.494 23.483 8.123   1.00 53.33 ? 240 LEU   B O    1 
ATOM   3752 C  CB   . LEU   B 1 209 ? -17.022 25.571 10.288  1.00 50.20 ? 240 LEU   B CB   1 
ATOM   3753 C  CG   . LEU   B 1 209 ? -16.795 26.295 8.950   1.00 48.43 ? 240 LEU   B CG   1 
ATOM   3754 C  CD1  . LEU   B 1 209 ? -18.090 26.891 8.395   1.00 42.85 ? 240 LEU   B CD1  1 
ATOM   3755 C  CD2  . LEU   B 1 209 ? -15.720 27.375 9.086   1.00 45.07 ? 240 LEU   B CD2  1 
ATOM   3756 N  N    . LYS   B 1 210 ? -16.868 22.559 9.385   1.00 53.11 ? 241 LYS   B N    1 
ATOM   3757 C  CA   . LYS   B 1 210 ? -16.557 21.565 8.361   1.00 53.07 ? 241 LYS   B CA   1 
ATOM   3758 C  C    . LYS   B 1 210 ? -17.733 20.623 8.124   1.00 53.02 ? 241 LYS   B C    1 
ATOM   3759 O  O    . LYS   B 1 210 ? -18.048 20.294 6.973   1.00 52.04 ? 241 LYS   B O    1 
ATOM   3760 C  CB   . LYS   B 1 210 ? -15.299 20.785 8.744   1.00 55.72 ? 241 LYS   B CB   1 
ATOM   3761 C  CG   . LYS   B 1 210 ? -14.900 19.735 7.717   1.00 58.73 ? 241 LYS   B CG   1 
ATOM   3762 C  CD   . LYS   B 1 210 ? -13.503 19.177 7.972   1.00 62.39 ? 241 LYS   B CD   1 
ATOM   3763 C  CE   . LYS   B 1 210 ? -13.245 17.947 7.096   1.00 63.03 ? 241 LYS   B CE   1 
ATOM   3764 N  NZ   . LYS   B 1 210 ? -11.823 17.491 7.144   1.00 64.67 ? 241 LYS   B NZ   1 
ATOM   3765 N  N    . LYS   B 1 211 ? -18.410 20.190 9.197   1.00 48.93 ? 242 LYS   B N    1 
ATOM   3766 C  CA   . LYS   B 1 211 ? -19.551 19.292 9.021   1.00 51.40 ? 242 LYS   B CA   1 
ATOM   3767 C  C    . LYS   B 1 211 ? -20.666 19.926 8.198   1.00 52.19 ? 242 LYS   B C    1 
ATOM   3768 O  O    . LYS   B 1 211 ? -21.467 19.201 7.596   1.00 55.57 ? 242 LYS   B O    1 
ATOM   3769 C  CB   . LYS   B 1 211 ? -20.102 18.840 10.378  1.00 57.77 ? 242 LYS   B CB   1 
ATOM   3770 C  CG   . LYS   B 1 211 ? -19.307 17.728 11.034  1.00 57.81 ? 242 LYS   B CG   1 
ATOM   3771 C  CD   . LYS   B 1 211 ? -20.008 17.201 12.276  1.00 63.02 ? 242 LYS   B CD   1 
ATOM   3772 C  CE   . LYS   B 1 211 ? -19.235 16.039 12.886  1.00 68.97 ? 242 LYS   B CE   1 
ATOM   3773 N  NZ   . LYS   B 1 211 ? -17.834 16.428 13.226  1.00 72.68 ? 242 LYS   B NZ   1 
ATOM   3774 N  N    . HIS   B 1 212 ? -20.730 21.257 8.143   1.00 50.57 ? 243 HIS   B N    1 
ATOM   3775 C  CA   . HIS   B 1 212 ? -21.727 21.924 7.311   1.00 49.98 ? 243 HIS   B CA   1 
ATOM   3776 C  C    . HIS   B 1 212 ? -21.203 22.283 5.919   1.00 49.19 ? 243 HIS   B C    1 
ATOM   3777 O  O    . HIS   B 1 212 ? -21.961 22.238 4.943   1.00 48.76 ? 243 HIS   B O    1 
ATOM   3778 C  CB   . HIS   B 1 212 ? -22.228 23.193 8.004   1.00 48.80 ? 243 HIS   B CB   1 
ATOM   3779 C  CG   . HIS   B 1 212 ? -23.063 22.937 9.220   1.00 50.88 ? 243 HIS   B CG   1 
ATOM   3780 N  ND1  . HIS   B 1 212 ? -22.553 22.998 10.498  1.00 50.32 ? 243 HIS   B ND1  1 
ATOM   3781 C  CD2  . HIS   B 1 212 ? -24.378 22.639 9.354   1.00 47.73 ? 243 HIS   B CD2  1 
ATOM   3782 C  CE1  . HIS   B 1 212 ? -23.515 22.750 11.370  1.00 52.54 ? 243 HIS   B CE1  1 
ATOM   3783 N  NE2  . HIS   B 1 212 ? -24.632 22.527 10.701  1.00 51.92 ? 243 HIS   B NE2  1 
ATOM   3784 N  N    . THR   B 1 213 ? -19.929 22.665 5.804   1.00 50.55 ? 244 THR   B N    1 
ATOM   3785 C  CA   . THR   B 1 213 ? -19.396 23.032 4.491   1.00 51.01 ? 244 THR   B CA   1 
ATOM   3786 C  C    . THR   B 1 213 ? -19.320 21.828 3.559   1.00 54.72 ? 244 THR   B C    1 
ATOM   3787 O  O    . THR   B 1 213 ? -19.544 21.964 2.346   1.00 48.14 ? 244 THR   B O    1 
ATOM   3788 C  CB   . THR   B 1 213 ? -18.020 23.677 4.631   1.00 51.47 ? 244 THR   B CB   1 
ATOM   3789 O  OG1  . THR   B 1 213 ? -17.179 22.837 5.431   1.00 55.28 ? 244 THR   B OG1  1 
ATOM   3790 C  CG2  . THR   B 1 213 ? -18.128 25.058 5.282   1.00 49.89 ? 244 THR   B CG2  1 
ATOM   3791 N  N    . ILE   B 1 214 ? -19.020 20.639 4.103   1.00 53.18 ? 245 ILE   B N    1 
ATOM   3792 C  CA   . ILE   B 1 214 ? -18.891 19.443 3.270   1.00 53.29 ? 245 ILE   B CA   1 
ATOM   3793 C  C    . ILE   B 1 214 ? -20.196 19.099 2.583   1.00 51.85 ? 245 ILE   B C    1 
ATOM   3794 O  O    . ILE   B 1 214 ? -20.193 18.394 1.571   1.00 56.74 ? 245 ILE   B O    1 
ATOM   3795 C  CB   . ILE   B 1 214 ? -18.392 18.227 4.081   1.00 53.91 ? 245 ILE   B CB   1 
ATOM   3796 C  CG1  . ILE   B 1 214 ? -19.473 17.741 5.053   1.00 56.55 ? 245 ILE   B CG1  1 
ATOM   3797 C  CG2  . ILE   B 1 214 ? -17.090 18.555 4.802   1.00 57.20 ? 245 ILE   B CG2  1 
ATOM   3798 C  CD1  . ILE   B 1 214 ? -19.165 16.392 5.679   1.00 61.26 ? 245 ILE   B CD1  1 
ATOM   3799 N  N    . LEU   B 1 215 ? -21.320 19.573 3.112   1.00 52.57 ? 246 LEU   B N    1 
ATOM   3800 C  CA   . LEU   B 1 215 ? -22.606 19.410 2.452   1.00 52.85 ? 246 LEU   B CA   1 
ATOM   3801 C  C    . LEU   B 1 215 ? -22.931 20.544 1.495   1.00 49.47 ? 246 LEU   B C    1 
ATOM   3802 O  O    . LEU   B 1 215 ? -23.954 20.472 0.806   1.00 52.21 ? 246 LEU   B O    1 
ATOM   3803 C  CB   . LEU   B 1 215 ? -23.730 19.321 3.490   1.00 54.88 ? 246 LEU   B CB   1 
ATOM   3804 C  CG   . LEU   B 1 215 ? -23.630 18.280 4.601   1.00 55.71 ? 246 LEU   B CG   1 
ATOM   3805 C  CD1  . LEU   B 1 215 ? -24.856 18.383 5.479   1.00 57.89 ? 246 LEU   B CD1  1 
ATOM   3806 C  CD2  . LEU   B 1 215 ? -23.513 16.885 4.020   1.00 59.35 ? 246 LEU   B CD2  1 
ATOM   3807 N  N    . ALA   B 1 216 ? -22.100 21.582 1.433   1.00 49.22 ? 247 ALA   B N    1 
ATOM   3808 C  CA   . ALA   B 1 216 ? -22.480 22.835 0.790   1.00 49.59 ? 247 ALA   B CA   1 
ATOM   3809 C  C    . ALA   B 1 216 ? -22.200 22.812 -0.708  1.00 49.94 ? 247 ALA   B C    1 
ATOM   3810 O  O    . ALA   B 1 216 ? -21.083 22.501 -1.138  1.00 49.80 ? 247 ALA   B O    1 
ATOM   3811 C  CB   . ALA   B 1 216 ? -21.744 24.014 1.428   1.00 45.41 ? 247 ALA   B CB   1 
ATOM   3812 N  N    . ASP   B 1 217 ? -23.217 23.166 -1.493  1.00 47.60 ? 248 ASP   B N    1 
ATOM   3813 C  CA   . ASP   B 1 217 ? -23.006 23.451 -2.902  1.00 48.33 ? 248 ASP   B CA   1 
ATOM   3814 C  C    . ASP   B 1 217 ? -22.303 24.783 -3.115  1.00 53.44 ? 248 ASP   B C    1 
ATOM   3815 O  O    . ASP   B 1 217 ? -21.687 24.987 -4.170  1.00 49.61 ? 248 ASP   B O    1 
ATOM   3816 C  CB   . ASP   B 1 217 ? -24.340 23.457 -3.634  1.00 52.22 ? 248 ASP   B CB   1 
ATOM   3817 C  CG   . ASP   B 1 217 ? -25.129 22.204 -3.387  1.00 55.25 ? 248 ASP   B CG   1 
ATOM   3818 O  OD1  . ASP   B 1 217 ? -26.105 22.264 -2.608  1.00 53.94 ? 248 ASP   B OD1  1 
ATOM   3819 O  OD2  . ASP   B 1 217 ? -24.757 21.158 -3.960  1.00 57.78 ? 248 ASP   B OD2  1 
ATOM   3820 N  N    . ILE   B 1 218 ? -22.425 25.713 -2.159  1.00 46.40 ? 249 ILE   B N    1 
ATOM   3821 C  CA   . ILE   B 1 218 ? -21.849 27.055 -2.254  1.00 45.11 ? 249 ILE   B CA   1 
ATOM   3822 C  C    . ILE   B 1 218 ? -21.350 27.455 -0.873  1.00 44.83 ? 249 ILE   B C    1 
ATOM   3823 O  O    . ILE   B 1 218 ? -22.129 27.474 0.086   1.00 44.80 ? 249 ILE   B O    1 
ATOM   3824 C  CB   . ILE   B 1 218 ? -22.855 28.108 -2.765  1.00 44.44 ? 249 ILE   B CB   1 
ATOM   3825 C  CG1  . ILE   B 1 218 ? -23.555 27.653 -4.044  1.00 43.92 ? 249 ILE   B CG1  1 
ATOM   3826 C  CG2  . ILE   B 1 218 ? -22.158 29.432 -3.003  1.00 43.88 ? 249 ILE   B CG2  1 
ATOM   3827 C  CD1  . ILE   B 1 218 ? -24.581 28.618 -4.546  1.00 42.02 ? 249 ILE   B CD1  1 
ATOM   3828 N  N    . VAL   B 1 219 ? -20.065 27.770 -0.762  1.00 44.25 ? 250 VAL   B N    1 
ATOM   3829 C  CA   . VAL   B 1 219 ? -19.486 28.269 0.479   1.00 42.37 ? 250 VAL   B CA   1 
ATOM   3830 C  C    . VAL   B 1 219 ? -19.062 29.713 0.253   1.00 47.27 ? 250 VAL   B C    1 
ATOM   3831 O  O    . VAL   B 1 219 ? -18.330 30.013 -0.702  1.00 45.75 ? 250 VAL   B O    1 
ATOM   3832 C  CB   . VAL   B 1 219 ? -18.304 27.406 0.952   1.00 45.65 ? 250 VAL   B CB   1 
ATOM   3833 C  CG1  . VAL   B 1 219 ? -17.676 28.015 2.204   1.00 39.97 ? 250 VAL   B CG1  1 
ATOM   3834 C  CG2  . VAL   B 1 219 ? -18.769 25.986 1.248   1.00 47.34 ? 250 VAL   B CG2  1 
ATOM   3835 N  N    . ILE   B 1 220 ? -19.539 30.605 1.119   1.00 41.66 ? 251 ILE   B N    1 
ATOM   3836 C  CA   . ILE   B 1 220 ? -19.310 32.042 1.025   1.00 38.53 ? 251 ILE   B CA   1 
ATOM   3837 C  C    . ILE   B 1 220 ? -18.628 32.474 2.312   1.00 45.17 ? 251 ILE   B C    1 
ATOM   3838 O  O    . ILE   B 1 220 ? -19.235 32.426 3.396   1.00 44.50 ? 251 ILE   B O    1 
ATOM   3839 C  CB   . ILE   B 1 220 ? -20.622 32.809 0.815   1.00 39.32 ? 251 ILE   B CB   1 
ATOM   3840 C  CG1  . ILE   B 1 220 ? -21.375 32.217 -0.366  1.00 41.96 ? 251 ILE   B CG1  1 
ATOM   3841 C  CG2  . ILE   B 1 220 ? -20.363 34.298 0.617   1.00 38.86 ? 251 ILE   B CG2  1 
ATOM   3842 C  CD1  . ILE   B 1 220 ? -22.774 32.685 -0.490  1.00 39.73 ? 251 ILE   B CD1  1 
ATOM   3843 N  N    . SER   B 1 221 ? -17.375 32.901 2.212   1.00 41.26 ? 252 SER   B N    1 
ATOM   3844 C  CA   . SER   B 1 221 ? -16.596 33.186 3.409   1.00 41.40 ? 252 SER   B CA   1 
ATOM   3845 C  C    . SER   B 1 221 ? -16.404 34.687 3.551   1.00 47.27 ? 252 SER   B C    1 
ATOM   3846 O  O    . SER   B 1 221 ? -15.780 35.319 2.693   1.00 42.95 ? 252 SER   B O    1 
ATOM   3847 C  CB   . SER   B 1 221 ? -15.251 32.473 3.380   1.00 47.69 ? 252 SER   B CB   1 
ATOM   3848 O  OG   . SER   B 1 221 ? -14.706 32.426 4.686   1.00 47.60 ? 252 SER   B OG   1 
ATOM   3849 N  N    . ALA   B 1 222 ? -16.920 35.246 4.646   1.00 42.41 ? 253 ALA   B N    1 
ATOM   3850 C  CA   . ALA   B 1 222 ? -16.888 36.678 4.895   1.00 42.14 ? 253 ALA   B CA   1 
ATOM   3851 C  C    . ALA   B 1 222 ? -16.456 36.941 6.322   1.00 45.02 ? 253 ALA   B C    1 
ATOM   3852 O  O    . ALA   B 1 222 ? -17.068 37.721 7.055   1.00 45.55 ? 253 ALA   B O    1 
ATOM   3853 C  CB   . ALA   B 1 222 ? -18.242 37.305 4.586   1.00 40.13 ? 253 ALA   B CB   1 
ATOM   3854 N  N    . ALA   B 1 223 ? -15.384 36.269 6.739   1.00 43.66 ? 254 ALA   B N    1 
ATOM   3855 C  CA   . ALA   B 1 223 ? -14.945 36.291 8.131   1.00 46.58 ? 254 ALA   B CA   1 
ATOM   3856 C  C    . ALA   B 1 223 ? -13.690 37.112 8.369   1.00 48.80 ? 254 ALA   B C    1 
ATOM   3857 O  O    . ALA   B 1 223 ? -13.496 37.605 9.482   1.00 44.41 ? 254 ALA   B O    1 
ATOM   3858 C  CB   . ALA   B 1 223 ? -14.700 34.863 8.639   1.00 43.85 ? 254 ALA   B CB   1 
ATOM   3859 N  N    . GLY   B 1 224 ? -12.851 37.290 7.353   1.00 51.96 ? 255 GLY   B N    1 
ATOM   3860 C  CA   . GLY   B 1 224 ? -11.584 37.974 7.542   1.00 51.87 ? 255 GLY   B CA   1 
ATOM   3861 C  C    . GLY   B 1 224 ? -10.533 37.143 8.244   1.00 51.79 ? 255 GLY   B C    1 
ATOM   3862 O  O    . GLY   B 1 224 ? -9.796  37.669 9.088   1.00 44.86 ? 255 GLY   B O    1 
ATOM   3863 N  N    . ILE   B 1 225 ? -10.436 35.859 7.902   1.00 55.12 ? 256 ILE   B N    1 
ATOM   3864 C  CA   . ILE   B 1 225 ? -9.516  34.905 8.519   1.00 54.89 ? 256 ILE   B CA   1 
ATOM   3865 C  C    . ILE   B 1 225 ? -8.810  34.124 7.414   1.00 55.50 ? 256 ILE   B C    1 
ATOM   3866 O  O    . ILE   B 1 225 ? -9.466  33.352 6.701   1.00 55.20 ? 256 ILE   B O    1 
ATOM   3867 C  CB   . ILE   B 1 225 ? -10.263 33.946 9.459   1.00 53.16 ? 256 ILE   B CB   1 
ATOM   3868 C  CG1  . ILE   B 1 225 ? -10.806 34.688 10.686  1.00 49.15 ? 256 ILE   B CG1  1 
ATOM   3869 C  CG2  . ILE   B 1 225 ? -9.372  32.785 9.862   1.00 50.69 ? 256 ILE   B CG2  1 
ATOM   3870 C  CD1  . ILE   B 1 225 ? -11.671 33.818 11.550  1.00 49.40 ? 256 ILE   B CD1  1 
ATOM   3871 N  N    . PRO   B 1 226 ? -7.496  34.273 7.236   1.00 55.54 ? 257 PRO   B N    1 
ATOM   3872 C  CA   . PRO   B 1 226 ? -6.813  33.516 6.174   1.00 57.18 ? 257 PRO   B CA   1 
ATOM   3873 C  C    . PRO   B 1 226 ? -6.929  32.009 6.374   1.00 55.05 ? 257 PRO   B C    1 
ATOM   3874 O  O    . PRO   B 1 226 ? -6.870  31.502 7.496   1.00 55.75 ? 257 PRO   B O    1 
ATOM   3875 C  CB   . PRO   B 1 226 ? -5.358  33.988 6.283   1.00 54.93 ? 257 PRO   B CB   1 
ATOM   3876 C  CG   . PRO   B 1 226 ? -5.445  35.322 6.926   1.00 55.72 ? 257 PRO   B CG   1 
ATOM   3877 C  CD   . PRO   B 1 226 ? -6.598  35.234 7.896   1.00 51.75 ? 257 PRO   B CD   1 
ATOM   3878 N  N    . ASN   B 1 227 ? -7.115  31.297 5.262   1.00 57.33 ? 258 ASN   B N    1 
ATOM   3879 C  CA   . ASN   B 1 227 ? -7.150  29.833 5.222   1.00 61.78 ? 258 ASN   B CA   1 
ATOM   3880 C  C    . ASN   B 1 227 ? -8.265  29.232 6.080   1.00 63.33 ? 258 ASN   B C    1 
ATOM   3881 O  O    . ASN   B 1 227 ? -8.180  28.064 6.481   1.00 59.72 ? 258 ASN   B O    1 
ATOM   3882 C  CB   . ASN   B 1 227 ? -5.794  29.240 5.631   1.00 65.09 ? 258 ASN   B CB   1 
ATOM   3883 C  CG   . ASN   B 1 227 ? -4.680  29.631 4.677   1.00 61.18 ? 258 ASN   B CG   1 
ATOM   3884 O  OD1  . ASN   B 1 227 ? -4.795  29.446 3.470   1.00 57.88 ? 258 ASN   B OD1  1 
ATOM   3885 N  ND2  . ASN   B 1 227 ? -3.611  30.204 5.216   1.00 64.15 ? 258 ASN   B ND2  1 
ATOM   3886 N  N    . LEU   B 1 228 ? -9.324  29.995 6.357   1.00 57.84 ? 259 LEU   B N    1 
ATOM   3887 C  CA   . LEU   B 1 228 ? -10.467 29.428 7.063   1.00 57.21 ? 259 LEU   B CA   1 
ATOM   3888 C  C    . LEU   B 1 228 ? -11.112 28.313 6.254   1.00 56.79 ? 259 LEU   B C    1 
ATOM   3889 O  O    . LEU   B 1 228 ? -11.637 27.351 6.825   1.00 60.38 ? 259 LEU   B O    1 
ATOM   3890 C  CB   . LEU   B 1 228 ? -11.485 30.527 7.369   1.00 55.51 ? 259 LEU   B CB   1 
ATOM   3891 C  CG   . LEU   B 1 228 ? -12.725 30.162 8.184   1.00 54.24 ? 259 LEU   B CG   1 
ATOM   3892 C  CD1  . LEU   B 1 228 ? -12.349 29.920 9.635   1.00 47.75 ? 259 LEU   B CD1  1 
ATOM   3893 C  CD2  . LEU   B 1 228 ? -13.777 31.261 8.062   1.00 49.80 ? 259 LEU   B CD2  1 
ATOM   3894 N  N    . ILE   B 1 229 ? -11.078 28.418 4.933   1.00 54.32 ? 260 ILE   B N    1 
ATOM   3895 C  CA   . ILE   B 1 229 ? -11.684 27.439 4.038   1.00 58.57 ? 260 ILE   B CA   1 
ATOM   3896 C  C    . ILE   B 1 229 ? -10.561 26.672 3.350   1.00 60.49 ? 260 ILE   B C    1 
ATOM   3897 O  O    . ILE   B 1 229 ? -9.782  27.255 2.585   1.00 60.41 ? 260 ILE   B O    1 
ATOM   3898 C  CB   . ILE   B 1 229 ? -12.597 28.113 3.004   1.00 53.31 ? 260 ILE   B CB   1 
ATOM   3899 C  CG1  . ILE   B 1 229 ? -13.547 29.109 3.685   1.00 54.00 ? 260 ILE   B CG1  1 
ATOM   3900 C  CG2  . ILE   B 1 229 ? -13.347 27.068 2.220   1.00 52.18 ? 260 ILE   B CG2  1 
ATOM   3901 C  CD1  . ILE   B 1 229 ? -14.391 28.513 4.805   1.00 47.46 ? 260 ILE   B CD1  1 
ATOM   3902 N  N    . THR   B 1 230 ? -10.472 25.369 3.620   1.00 59.69 ? 261 THR   B N    1 
ATOM   3903 C  CA   . THR   B 1 230 ? -9.474  24.510 3.001   1.00 57.97 ? 261 THR   B CA   1 
ATOM   3904 C  C    . THR   B 1 230 ? -10.170 23.342 2.317   1.00 61.57 ? 261 THR   B C    1 
ATOM   3905 O  O    . THR   B 1 230 ? -11.341 23.051 2.579   1.00 61.26 ? 261 THR   B O    1 
ATOM   3906 C  CB   . THR   B 1 230 ? -8.445  23.997 4.014   1.00 61.17 ? 261 THR   B CB   1 
ATOM   3907 O  OG1  . THR   B 1 230 ? -9.089  23.143 4.966   1.00 64.94 ? 261 THR   B OG1  1 
ATOM   3908 C  CG2  . THR   B 1 230 ? -7.784  25.158 4.743   1.00 57.42 ? 261 THR   B CG2  1 
ATOM   3909 N  N    . ALA   B 1 231 ? -9.425  22.675 1.426   1.00 62.57 ? 262 ALA   B N    1 
ATOM   3910 C  CA   . ALA   B 1 231 ? -10.035 21.738 0.486   1.00 60.55 ? 262 ALA   B CA   1 
ATOM   3911 C  C    . ALA   B 1 231 ? -10.783 20.611 1.188   1.00 58.78 ? 262 ALA   B C    1 
ATOM   3912 O  O    . ALA   B 1 231 ? -11.806 20.139 0.673   1.00 60.96 ? 262 ALA   B O    1 
ATOM   3913 C  CB   . ALA   B 1 231 ? -8.972  21.163 -0.453  1.00 61.69 ? 262 ALA   B CB   1 
ATOM   3914 N  N    . ASP   B 1 232 ? -10.305 20.173 2.358   1.00 59.69 ? 263 ASP   B N    1 
ATOM   3915 C  CA   . ASP   B 1 232 ? -10.989 19.108 3.087   1.00 64.04 ? 263 ASP   B CA   1 
ATOM   3916 C  C    . ASP   B 1 232 ? -12.387 19.511 3.546   1.00 63.66 ? 263 ASP   B C    1 
ATOM   3917 O  O    . ASP   B 1 232 ? -13.183 18.637 3.905   1.00 62.90 ? 263 ASP   B O    1 
ATOM   3918 C  CB   . ASP   B 1 232 ? -10.169 18.670 4.303   1.00 62.75 ? 263 ASP   B CB   1 
ATOM   3919 C  CG   . ASP   B 1 232 ? -9.801  19.829 5.206   1.00 64.31 ? 263 ASP   B CG   1 
ATOM   3920 O  OD1  . ASP   B 1 232 ? -9.136  20.766 4.716   1.00 65.12 ? 263 ASP   B OD1  1 
ATOM   3921 O  OD2  . ASP   B 1 232 ? -10.182 19.814 6.398   1.00 64.95 ? 263 ASP   B OD2  1 
ATOM   3922 N  N    . MET   B 1 233 ? -12.701 20.806 3.561   1.00 62.32 ? 264 MET   B N    1 
ATOM   3923 C  CA   . MET   B 1 233 ? -14.022 21.255 3.983   1.00 58.77 ? 264 MET   B CA   1 
ATOM   3924 C  C    . MET   B 1 233 ? -15.010 21.395 2.834   1.00 59.85 ? 264 MET   B C    1 
ATOM   3925 O  O    . MET   B 1 233 ? -16.198 21.604 3.095   1.00 54.65 ? 264 MET   B O    1 
ATOM   3926 C  CB   . MET   B 1 233 ? -13.918 22.596 4.714   1.00 53.28 ? 264 MET   B CB   1 
ATOM   3927 C  CG   . MET   B 1 233 ? -12.675 22.739 5.557   1.00 57.68 ? 264 MET   B CG   1 
ATOM   3928 S  SD   . MET   B 1 233 ? -12.561 24.406 6.206   1.00 57.19 ? 264 MET   B SD   1 
ATOM   3929 C  CE   . MET   B 1 233 ? -10.988 24.358 7.054   1.00 60.52 ? 264 MET   B CE   1 
ATOM   3930 N  N    . ILE   B 1 234 ? -14.563 21.266 1.582   1.00 56.71 ? 265 ILE   B N    1 
ATOM   3931 C  CA   . ILE   B 1 234 ? -15.359 21.626 0.413   1.00 54.36 ? 265 ILE   B CA   1 
ATOM   3932 C  C    . ILE   B 1 234 ? -15.828 20.366 -0.299  1.00 60.14 ? 265 ILE   B C    1 
ATOM   3933 O  O    . ILE   B 1 234 ? -15.041 19.443 -0.536  1.00 62.36 ? 265 ILE   B O    1 
ATOM   3934 C  CB   . ILE   B 1 234 ? -14.563 22.526 -0.548  1.00 54.99 ? 265 ILE   B CB   1 
ATOM   3935 C  CG1  . ILE   B 1 234 ? -14.124 23.798 0.171   1.00 57.65 ? 265 ILE   B CG1  1 
ATOM   3936 C  CG2  . ILE   B 1 234 ? -15.398 22.874 -1.763  1.00 56.54 ? 265 ILE   B CG2  1 
ATOM   3937 C  CD1  . ILE   B 1 234 ? -15.291 24.584 0.741   1.00 53.73 ? 265 ILE   B CD1  1 
ATOM   3938 N  N    . LYS   B 1 235 ? -17.111 20.333 -0.642  1.00 60.23 ? 266 LYS   B N    1 
ATOM   3939 C  CA   . LYS   B 1 235 ? -17.639 19.287 -1.506  1.00 59.90 ? 266 LYS   B CA   1 
ATOM   3940 C  C    . LYS   B 1 235 ? -17.037 19.431 -2.900  1.00 64.13 ? 266 LYS   B C    1 
ATOM   3941 O  O    . LYS   B 1 235 ? -16.939 20.545 -3.426  1.00 61.89 ? 266 LYS   B O    1 
ATOM   3942 C  CB   . LYS   B 1 235 ? -19.164 19.390 -1.563  1.00 60.44 ? 266 LYS   B CB   1 
ATOM   3943 C  CG   . LYS   B 1 235 ? -19.878 18.161 -2.071  1.00 59.72 ? 266 LYS   B CG   1 
ATOM   3944 C  CD   . LYS   B 1 235 ? -21.381 18.403 -2.138  1.00 58.68 ? 266 LYS   B CD   1 
ATOM   3945 C  CE   . LYS   B 1 235 ? -21.775 19.322 -3.285  1.00 64.41 ? 266 LYS   B CE   1 
ATOM   3946 N  NZ   . LYS   B 1 235 ? -22.569 18.615 -4.339  1.00 70.56 ? 266 LYS   B NZ   1 
ATOM   3947 N  N    . GLU   B 1 236 ? -16.606 18.315 -3.490  1.00 62.16 ? 267 GLU   B N    1 
ATOM   3948 C  CA   . GLU   B 1 236 ? -16.096 18.360 -4.854  1.00 64.29 ? 267 GLU   B CA   1 
ATOM   3949 C  C    . GLU   B 1 236 ? -17.142 18.949 -5.791  1.00 62.69 ? 267 GLU   B C    1 
ATOM   3950 O  O    . GLU   B 1 236 ? -18.301 18.527 -5.791  1.00 62.28 ? 267 GLU   B O    1 
ATOM   3951 C  CB   . GLU   B 1 236 ? -15.696 16.960 -5.327  1.00 68.21 ? 267 GLU   B CB   1 
ATOM   3952 C  CG   . GLU   B 1 236 ? -15.828 16.794 -6.832  1.00 74.25 ? 267 GLU   B CG   1 
ATOM   3953 C  CD   . GLU   B 1 236 ? -14.974 15.680 -7.402  1.00 84.27 ? 267 GLU   B CD   1 
ATOM   3954 O  OE1  . GLU   B 1 236 ? -15.520 14.586 -7.666  1.00 84.42 ? 267 GLU   B OE1  1 
ATOM   3955 O  OE2  . GLU   B 1 236 ? -13.761 15.911 -7.602  1.00 87.98 ? 267 GLU   B OE2  1 
ATOM   3956 N  N    . GLY   B 1 237 ? -16.722 19.934 -6.592  1.00 59.58 ? 268 GLY   B N    1 
ATOM   3957 C  CA   . GLY   B 1 237 ? -17.612 20.616 -7.505  1.00 58.37 ? 268 GLY   B CA   1 
ATOM   3958 C  C    . GLY   B 1 237 ? -18.320 21.832 -6.941  1.00 59.25 ? 268 GLY   B C    1 
ATOM   3959 O  O    . GLY   B 1 237 ? -19.031 22.519 -7.692  1.00 55.64 ? 268 GLY   B O    1 
ATOM   3960 N  N    . ALA   B 1 238 ? -18.153 22.124 -5.653  1.00 57.59 ? 269 ALA   B N    1 
ATOM   3961 C  CA   . ALA   B 1 238 ? -18.857 23.242 -5.041  1.00 55.75 ? 269 ALA   B CA   1 
ATOM   3962 C  C    . ALA   B 1 238 ? -18.343 24.574 -5.583  1.00 56.66 ? 269 ALA   B C    1 
ATOM   3963 O  O    . ALA   B 1 238 ? -17.241 24.676 -6.138  1.00 56.81 ? 269 ALA   B O    1 
ATOM   3964 C  CB   . ALA   B 1 238 ? -18.702 23.210 -3.516  1.00 53.61 ? 269 ALA   B CB   1 
ATOM   3965 N  N    . ALA   B 1 239 ? -19.174 25.604 -5.431  1.00 52.18 ? 270 ALA   B N    1 
ATOM   3966 C  CA   . ALA   B 1 239 ? -18.775 26.980 -5.696  1.00 48.55 ? 270 ALA   B CA   1 
ATOM   3967 C  C    . ALA   B 1 239 ? -18.305 27.627 -4.399  1.00 50.38 ? 270 ALA   B C    1 
ATOM   3968 O  O    . ALA   B 1 239 ? -18.983 27.529 -3.365  1.00 46.75 ? 270 ALA   B O    1 
ATOM   3969 C  CB   . ALA   B 1 239 ? -19.933 27.775 -6.303  1.00 44.77 ? 270 ALA   B CB   1 
ATOM   3970 N  N    . VAL   B 1 240 ? -17.143 28.271 -4.445  1.00 43.74 ? 271 VAL   B N    1 
ATOM   3971 C  CA   . VAL   B 1 240 ? -16.562 28.918 -3.272  1.00 43.14 ? 271 VAL   B CA   1 
ATOM   3972 C  C    . VAL   B 1 240 ? -16.350 30.391 -3.589  1.00 47.83 ? 271 VAL   B C    1 
ATOM   3973 O  O    . VAL   B 1 240 ? -15.577 30.731 -4.494  1.00 46.21 ? 271 VAL   B O    1 
ATOM   3974 C  CB   . VAL   B 1 240 ? -15.246 28.254 -2.850  1.00 46.54 ? 271 VAL   B CB   1 
ATOM   3975 C  CG1  . VAL   B 1 240 ? -14.640 28.995 -1.666  1.00 44.42 ? 271 VAL   B CG1  1 
ATOM   3976 C  CG2  . VAL   B 1 240 ? -15.492 26.807 -2.493  1.00 48.86 ? 271 VAL   B CG2  1 
ATOM   3977 N  N    . ILE   B 1 241 ? -17.020 31.261 -2.835  1.00 47.49 ? 272 ILE   B N    1 
ATOM   3978 C  CA   . ILE   B 1 241 ? -16.974 32.709 -3.027  1.00 44.03 ? 272 ILE   B CA   1 
ATOM   3979 C  C    . ILE   B 1 241 ? -16.246 33.314 -1.838  1.00 45.16 ? 272 ILE   B C    1 
ATOM   3980 O  O    . ILE   B 1 241 ? -16.717 33.210 -0.696  1.00 44.12 ? 272 ILE   B O    1 
ATOM   3981 C  CB   . ILE   B 1 241 ? -18.380 33.318 -3.151  1.00 42.37 ? 272 ILE   B CB   1 
ATOM   3982 C  CG1  . ILE   B 1 241 ? -19.298 32.475 -4.051  1.00 44.33 ? 272 ILE   B CG1  1 
ATOM   3983 C  CG2  . ILE   B 1 241 ? -18.287 34.757 -3.622  1.00 43.89 ? 272 ILE   B CG2  1 
ATOM   3984 C  CD1  . ILE   B 1 241 ? -18.955 32.501 -5.490  1.00 46.56 ? 272 ILE   B CD1  1 
ATOM   3985 N  N    . ASP   B 1 242 ? -15.138 34.002 -2.104  1.00 44.71 ? 273 ASP   B N    1 
ATOM   3986 C  CA   . ASP   B 1 242 ? -14.236 34.485 -1.062  1.00 43.87 ? 273 ASP   B CA   1 
ATOM   3987 C  C    . ASP   B 1 242 ? -14.402 35.990 -0.870  1.00 45.62 ? 273 ASP   B C    1 
ATOM   3988 O  O    . ASP   B 1 242 ? -13.906 36.782 -1.677  1.00 42.33 ? 273 ASP   B O    1 
ATOM   3989 C  CB   . ASP   B 1 242 ? -12.796 34.143 -1.426  1.00 46.59 ? 273 ASP   B CB   1 
ATOM   3990 C  CG   . ASP   B 1 242 ? -11.852 34.269 -0.259  1.00 51.17 ? 273 ASP   B CG   1 
ATOM   3991 O  OD1  . ASP   B 1 242 ? -12.196 34.934 0.754   1.00 49.01 ? 273 ASP   B OD1  1 
ATOM   3992 O  OD2  . ASP   B 1 242 ? -10.745 33.701 -0.366  1.00 53.00 ? 273 ASP   B OD2  1 
ATOM   3993 N  N    . VAL   B 1 243 ? -15.052 36.386 0.226   1.00 41.83 ? 274 VAL   B N    1 
ATOM   3994 C  CA   . VAL   B 1 243 ? -15.298 37.803 0.478   1.00 42.64 ? 274 VAL   B CA   1 
ATOM   3995 C  C    . VAL   B 1 243 ? -14.188 38.457 1.300   1.00 45.39 ? 274 VAL   B C    1 
ATOM   3996 O  O    . VAL   B 1 243 ? -13.974 39.667 1.182   1.00 50.41 ? 274 VAL   B O    1 
ATOM   3997 C  CB   . VAL   B 1 243 ? -16.668 37.990 1.166   1.00 43.06 ? 274 VAL   B CB   1 
ATOM   3998 C  CG1  . VAL   B 1 243 ? -17.019 39.474 1.353   1.00 41.63 ? 274 VAL   B CG1  1 
ATOM   3999 C  CG2  . VAL   B 1 243 ? -17.750 37.289 0.366   1.00 39.22 ? 274 VAL   B CG2  1 
ATOM   4000 N  N    . GLY   B 1 244 ? -13.446 37.695 2.091   1.00 45.91 ? 275 GLY   B N    1 
ATOM   4001 C  CA   . GLY   B 1 244 ? -12.437 38.300 2.939   1.00 51.38 ? 275 GLY   B CA   1 
ATOM   4002 C  C    . GLY   B 1 244 ? -11.302 38.920 2.144   1.00 52.33 ? 275 GLY   B C    1 
ATOM   4003 O  O    . GLY   B 1 244 ? -10.997 38.520 1.019   1.00 53.51 ? 275 GLY   B O    1 
ATOM   4004 N  N    . ILE   B 1 245 ? -10.676 39.929 2.746   1.00 54.18 ? 276 ILE   B N    1 
ATOM   4005 C  CA   . ILE   B 1 245 ? -9.485  40.578 2.205   1.00 57.22 ? 276 ILE   B CA   1 
ATOM   4006 C  C    . ILE   B 1 245 ? -8.497  40.704 3.363   1.00 60.61 ? 276 ILE   B C    1 
ATOM   4007 O  O    . ILE   B 1 245 ? -8.662  41.562 4.239   1.00 58.14 ? 276 ILE   B O    1 
ATOM   4008 C  CB   . ILE   B 1 245 ? -9.795  41.943 1.573   1.00 54.65 ? 276 ILE   B CB   1 
ATOM   4009 C  CG1  . ILE   B 1 245 ? -10.711 41.756 0.351   1.00 54.00 ? 276 ILE   B CG1  1 
ATOM   4010 C  CG2  . ILE   B 1 245 ? -8.513  42.650 1.170   1.00 59.84 ? 276 ILE   B CG2  1 
ATOM   4011 C  CD1  . ILE   B 1 245 ? -10.896 43.007 -0.507  1.00 51.20 ? 276 ILE   B CD1  1 
ATOM   4012 N  N    . ASN   B 1 246 ? -7.475  39.845 3.379   1.00 58.42 ? 277 ASN   B N    1 
ATOM   4013 C  CA   . ASN   B 1 246 ? -6.570  39.716 4.515   1.00 56.76 ? 277 ASN   B CA   1 
ATOM   4014 C  C    . ASN   B 1 246 ? -5.137  40.008 4.089   1.00 63.08 ? 277 ASN   B C    1 
ATOM   4015 O  O    . ASN   B 1 246 ? -4.686  39.540 3.036   1.00 66.37 ? 277 ASN   B O    1 
ATOM   4016 C  CB   . ASN   B 1 246 ? -6.647  38.308 5.108   1.00 57.96 ? 277 ASN   B CB   1 
ATOM   4017 C  CG   . ASN   B 1 246 ? -8.075  37.852 5.347   1.00 58.82 ? 277 ASN   B CG   1 
ATOM   4018 O  OD1  . ASN   B 1 246 ? -8.837  38.506 6.059   1.00 55.52 ? 277 ASN   B OD1  1 
ATOM   4019 N  ND2  . ASN   B 1 246 ? -8.448  36.725 4.741   1.00 56.00 ? 277 ASN   B ND2  1 
ATOM   4020 N  N    . ARG   B 1 247 ? -4.425  40.772 4.915   1.00 61.75 ? 278 ARG   B N    1 
ATOM   4021 C  CA   . ARG   B 1 247 ? -3.015  41.079 4.684   1.00 68.65 ? 278 ARG   B CA   1 
ATOM   4022 C  C    . ARG   B 1 247 ? -2.154  40.015 5.361   1.00 72.77 ? 278 ARG   B C    1 
ATOM   4023 O  O    . ARG   B 1 247 ? -2.078  39.957 6.592   1.00 69.56 ? 278 ARG   B O    1 
ATOM   4024 C  CB   . ARG   B 1 247 ? -2.672  42.472 5.205   1.00 66.99 ? 278 ARG   B CB   1 
ATOM   4025 N  N    . VAL   B 1 248 ? -1.491  39.214 4.535   1.00 75.51 ? 279 VAL   B N    1 
ATOM   4026 C  CA   . VAL   B 1 248 ? -0.571  38.185 5.077   1.00 76.28 ? 279 VAL   B CA   1 
ATOM   4027 C  C    . VAL   B 1 248 ? 0.778   38.352 4.393   1.00 82.51 ? 279 VAL   B C    1 
ATOM   4028 O  O    . VAL   B 1 248 ? 0.904   39.210 3.506   1.00 81.17 ? 279 VAL   B O    1 
ATOM   4029 C  CB   . VAL   B 1 248 ? -1.108  36.766 4.846   1.00 76.15 ? 279 VAL   B CB   1 
ATOM   4030 N  N    . HIS   B 1 249 ? 1.742   37.544 4.798   1.00 83.40 ? 280 HIS   B N    1 
ATOM   4031 C  CA   . HIS   B 1 249 ? 3.089   37.609 4.231   1.00 80.29 ? 280 HIS   B CA   1 
ATOM   4032 C  C    . HIS   B 1 249 ? 3.603   36.214 3.891   1.00 80.19 ? 280 HIS   B C    1 
ATOM   4033 O  O    . HIS   B 1 249 ? 3.738   35.858 2.718   1.00 83.18 ? 280 HIS   B O    1 
ATOM   4034 C  CB   . HIS   B 1 249 ? 4.048   38.306 5.199   1.00 80.03 ? 280 HIS   B CB   1 
ATOM   4035 N  N    . LYS   B 1 257 ? 1.214   40.997 1.190   1.00 72.69 ? 288 LYS   B N    1 
ATOM   4036 C  CA   . LYS   B 1 257 ? 0.402   40.251 0.228   1.00 73.91 ? 288 LYS   B CA   1 
ATOM   4037 C  C    . LYS   B 1 257 ? -1.060  40.172 0.679   1.00 74.53 ? 288 LYS   B C    1 
ATOM   4038 O  O    . LYS   B 1 257 ? -1.343  40.132 1.879   1.00 75.24 ? 288 LYS   B O    1 
ATOM   4039 C  CB   . LYS   B 1 257 ? 0.970   38.842 0.031   1.00 72.74 ? 288 LYS   B CB   1 
ATOM   4040 C  CG   . LYS   B 1 257 ? 0.243   38.028 -1.026  1.00 71.51 ? 288 LYS   B CG   1 
ATOM   4041 C  CD   . LYS   B 1 257 ? 0.770   36.605 -1.121  1.00 72.38 ? 288 LYS   B CD   1 
ATOM   4042 C  CE   . LYS   B 1 257 ? 0.621   35.870 0.194   1.00 75.02 ? 288 LYS   B CE   1 
ATOM   4043 N  NZ   . LYS   B 1 257 ? 0.554   34.394 -0.009  1.00 77.05 ? 288 LYS   B NZ   1 
ATOM   4044 N  N    . LEU   B 1 258 ? -1.991  40.152 -0.275  1.00 70.61 ? 289 LEU   B N    1 
ATOM   4045 C  CA   . LEU   B 1 258 ? -3.414  40.060 0.026   1.00 69.64 ? 289 LEU   B CA   1 
ATOM   4046 C  C    . LEU   B 1 258 ? -3.940  38.675 -0.322  1.00 65.75 ? 289 LEU   B C    1 
ATOM   4047 O  O    . LEU   B 1 258 ? -3.649  38.144 -1.401  1.00 65.41 ? 289 LEU   B O    1 
ATOM   4048 C  CB   . LEU   B 1 258 ? -4.221  41.115 -0.730  1.00 66.85 ? 289 LEU   B CB   1 
ATOM   4049 C  CG   . LEU   B 1 258 ? -4.142  42.570 -0.280  1.00 69.89 ? 289 LEU   B CG   1 
ATOM   4050 C  CD1  . LEU   B 1 258 ? -5.246  43.362 -0.980  1.00 71.97 ? 289 LEU   B CD1  1 
ATOM   4051 C  CD2  . LEU   B 1 258 ? -4.232  42.700 1.229   1.00 65.00 ? 289 LEU   B CD2  1 
ATOM   4052 N  N    . VAL   B 1 259 ? -4.715  38.097 0.597   1.00 61.52 ? 290 VAL   B N    1 
ATOM   4053 C  CA   . VAL   B 1 259 ? -5.409  36.837 0.375   1.00 60.94 ? 290 VAL   B CA   1 
ATOM   4054 C  C    . VAL   B 1 259 ? -6.805  36.944 0.976   1.00 58.34 ? 290 VAL   B C    1 
ATOM   4055 O  O    . VAL   B 1 259 ? -7.072  37.774 1.849   1.00 54.44 ? 290 VAL   B O    1 
ATOM   4056 C  CB   . VAL   B 1 259 ? -4.657  35.626 0.979   1.00 62.48 ? 290 VAL   B CB   1 
ATOM   4057 C  CG1  . VAL   B 1 259 ? -3.367  35.350 0.213   1.00 67.37 ? 290 VAL   B CG1  1 
ATOM   4058 C  CG2  . VAL   B 1 259 ? -4.368  35.859 2.457   1.00 61.31 ? 290 VAL   B CG2  1 
ATOM   4059 N  N    . GLY   B 1 260 ? -7.698  36.083 0.497   1.00 56.26 ? 291 GLY   B N    1 
ATOM   4060 C  CA   . GLY   B 1 260 ? -9.035  35.984 1.043   1.00 58.61 ? 291 GLY   B CA   1 
ATOM   4061 C  C    . GLY   B 1 260 ? -9.077  35.106 2.280   1.00 58.17 ? 291 GLY   B C    1 
ATOM   4062 O  O    . GLY   B 1 260 ? -8.075  34.906 2.973   1.00 55.27 ? 291 GLY   B O    1 
ATOM   4063 N  N    . ASP   B 1 261 ? -10.276 34.597 2.575   1.00 59.03 ? 292 ASP   B N    1 
ATOM   4064 C  CA   . ASP   B 1 261 ? -10.415 33.617 3.646   1.00 58.82 ? 292 ASP   B CA   1 
ATOM   4065 C  C    . ASP   B 1 261 ? -10.080 32.202 3.182   1.00 56.17 ? 292 ASP   B C    1 
ATOM   4066 O  O    . ASP   B 1 261 ? -9.893  31.314 4.022   1.00 56.59 ? 292 ASP   B O    1 
ATOM   4067 C  CB   . ASP   B 1 261 ? -11.841 33.638 4.214   1.00 54.07 ? 292 ASP   B CB   1 
ATOM   4068 C  CG   . ASP   B 1 261 ? -12.216 34.975 4.837   1.00 53.97 ? 292 ASP   B CG   1 
ATOM   4069 O  OD1  . ASP   B 1 261 ? -13.434 35.270 4.895   1.00 53.66 ? 292 ASP   B OD1  1 
ATOM   4070 O  OD2  . ASP   B 1 261 ? -11.309 35.731 5.258   1.00 53.74 ? 292 ASP   B OD2  1 
ATOM   4071 N  N    . VAL   B 1 262 ? -9.993  31.986 1.871   1.00 55.24 ? 293 VAL   B N    1 
ATOM   4072 C  CA   . VAL   B 1 262 ? -9.881  30.661 1.271   1.00 57.88 ? 293 VAL   B CA   1 
ATOM   4073 C  C    . VAL   B 1 262 ? -8.418  30.355 0.976   1.00 62.72 ? 293 VAL   B C    1 
ATOM   4074 O  O    . VAL   B 1 262 ? -7.661  31.230 0.535   1.00 62.21 ? 293 VAL   B O    1 
ATOM   4075 C  CB   . VAL   B 1 262 ? -10.730 30.571 -0.014  1.00 57.61 ? 293 VAL   B CB   1 
ATOM   4076 C  CG1  . VAL   B 1 262 ? -10.606 29.194 -0.666  1.00 54.37 ? 293 VAL   B CG1  1 
ATOM   4077 C  CG2  . VAL   B 1 262 ? -12.187 30.890 0.283   1.00 57.05 ? 293 VAL   B CG2  1 
ATOM   4078 N  N    . ASP   B 1 263 ? -8.013  29.109 1.229   1.00 64.35 ? 294 ASP   B N    1 
ATOM   4079 C  CA   . ASP   B 1 263 ? -6.745  28.607 0.713   1.00 63.65 ? 294 ASP   B CA   1 
ATOM   4080 C  C    . ASP   B 1 263 ? -6.928  28.420 -0.786  1.00 62.82 ? 294 ASP   B C    1 
ATOM   4081 O  O    . ASP   B 1 263 ? -7.428  27.381 -1.230  1.00 62.63 ? 294 ASP   B O    1 
ATOM   4082 C  CB   . ASP   B 1 263 ? -6.352  27.303 1.422   1.00 65.47 ? 294 ASP   B CB   1 
ATOM   4083 C  CG   . ASP   B 1 263 ? -5.228  26.540 0.713   1.00 68.33 ? 294 ASP   B CG   1 
ATOM   4084 O  OD1  . ASP   B 1 263 ? -4.518  27.115 -0.148  1.00 65.92 ? 294 ASP   B OD1  1 
ATOM   4085 O  OD2  . ASP   B 1 263 ? -5.059  25.339 1.032   1.00 65.74 ? 294 ASP   B OD2  1 
ATOM   4086 N  N    . PHE   B 1 264 ? -6.541  29.435 -1.567  1.00 62.53 ? 295 PHE   B N    1 
ATOM   4087 C  CA   . PHE   B 1 264 ? -6.915  29.479 -2.977  1.00 60.25 ? 295 PHE   B CA   1 
ATOM   4088 C  C    . PHE   B 1 264 ? -6.336  28.298 -3.751  1.00 63.15 ? 295 PHE   B C    1 
ATOM   4089 O  O    . PHE   B 1 264 ? -7.057  27.608 -4.484  1.00 62.24 ? 295 PHE   B O    1 
ATOM   4090 C  CB   . PHE   B 1 264 ? -6.469  30.804 -3.602  1.00 59.79 ? 295 PHE   B CB   1 
ATOM   4091 C  CG   . PHE   B 1 264 ? -6.958  30.996 -5.012  1.00 60.74 ? 295 PHE   B CG   1 
ATOM   4092 C  CD1  . PHE   B 1 264 ? -8.255  31.429 -5.258  1.00 54.55 ? 295 PHE   B CD1  1 
ATOM   4093 C  CD2  . PHE   B 1 264 ? -6.127  30.721 -6.095  1.00 61.98 ? 295 PHE   B CD2  1 
ATOM   4094 C  CE1  . PHE   B 1 264 ? -8.713  31.592 -6.556  1.00 57.45 ? 295 PHE   B CE1  1 
ATOM   4095 C  CE2  . PHE   B 1 264 ? -6.578  30.878 -7.396  1.00 64.74 ? 295 PHE   B CE2  1 
ATOM   4096 C  CZ   . PHE   B 1 264 ? -7.871  31.315 -7.631  1.00 61.47 ? 295 PHE   B CZ   1 
ATOM   4097 N  N    . GLU   B 1 265 ? -5.032  28.050 -3.608  1.00 63.09 ? 296 GLU   B N    1 
ATOM   4098 C  CA   . GLU   B 1 265 ? -4.406  27.029 -4.445  1.00 66.57 ? 296 GLU   B CA   1 
ATOM   4099 C  C    . GLU   B 1 265 ? -4.916  25.634 -4.096  1.00 68.80 ? 296 GLU   B C    1 
ATOM   4100 O  O    . GLU   B 1 265 ? -5.175  24.823 -4.996  1.00 68.18 ? 296 GLU   B O    1 
ATOM   4101 C  CB   . GLU   B 1 265 ? -2.882  27.114 -4.341  1.00 64.72 ? 296 GLU   B CB   1 
ATOM   4102 C  CG   . GLU   B 1 265 ? -2.276  28.334 -5.058  1.00 64.44 ? 296 GLU   B CG   1 
ATOM   4103 C  CD   . GLU   B 1 265 ? -2.713  28.464 -6.523  1.00 66.92 ? 296 GLU   B CD   1 
ATOM   4104 O  OE1  . GLU   B 1 265 ? -2.717  29.597 -7.052  1.00 67.93 ? 296 GLU   B OE1  1 
ATOM   4105 O  OE2  . GLU   B 1 265 ? -3.053  27.440 -7.152  1.00 70.33 ? 296 GLU   B OE2  1 
ATOM   4106 N  N    . GLY   B 1 266 ? -5.088  25.343 -2.802  1.00 66.10 ? 297 GLY   B N    1 
ATOM   4107 C  CA   . GLY   B 1 266 ? -5.644  24.054 -2.410  1.00 65.25 ? 297 GLY   B CA   1 
ATOM   4108 C  C    . GLY   B 1 266 ? -7.089  23.866 -2.846  1.00 67.92 ? 297 GLY   B C    1 
ATOM   4109 O  O    . GLY   B 1 266 ? -7.436  22.853 -3.463  1.00 69.52 ? 297 GLY   B O    1 
ATOM   4110 N  N    . VAL   B 1 267 ? -7.952  24.842 -2.537  1.00 64.99 ? 298 VAL   B N    1 
ATOM   4111 C  CA   . VAL   B 1 267 ? -9.377  24.710 -2.841  1.00 62.33 ? 298 VAL   B CA   1 
ATOM   4112 C  C    . VAL   B 1 267 ? -9.614  24.734 -4.344  1.00 64.24 ? 298 VAL   B C    1 
ATOM   4113 O  O    . VAL   B 1 267 ? -10.584 24.142 -4.840  1.00 63.13 ? 298 VAL   B O    1 
ATOM   4114 C  CB   . VAL   B 1 267 ? -10.176 25.806 -2.109  1.00 60.38 ? 298 VAL   B CB   1 
ATOM   4115 C  CG1  . VAL   B 1 267 ? -11.601 25.921 -2.657  1.00 54.47 ? 298 VAL   B CG1  1 
ATOM   4116 C  CG2  . VAL   B 1 267 ? -10.199 25.516 -0.609  1.00 60.91 ? 298 VAL   B CG2  1 
ATOM   4117 N  N    . ARG   B 1 268 ? -8.726  25.394 -5.092  1.00 65.27 ? 299 ARG   B N    1 
ATOM   4118 C  CA   . ARG   B 1 268 ? -8.807  25.395 -6.548  1.00 69.19 ? 299 ARG   B CA   1 
ATOM   4119 C  C    . ARG   B 1 268 ? -8.846  23.978 -7.111  1.00 71.13 ? 299 ARG   B C    1 
ATOM   4120 O  O    . ARG   B 1 268 ? -9.459  23.737 -8.158  1.00 70.83 ? 299 ARG   B O    1 
ATOM   4121 C  CB   . ARG   B 1 268 ? -7.609  26.168 -7.104  1.00 69.32 ? 299 ARG   B CB   1 
ATOM   4122 C  CG   . ARG   B 1 268 ? -7.408  26.111 -8.590  1.00 75.02 ? 299 ARG   B CG   1 
ATOM   4123 C  CD   . ARG   B 1 268 ? -6.151  26.878 -8.948  1.00 76.64 ? 299 ARG   B CD   1 
ATOM   4124 N  NE   . ARG   B 1 268 ? -6.248  27.487 -10.266 1.00 76.71 ? 299 ARG   B NE   1 
ATOM   4125 C  CZ   . ARG   B 1 268 ? -5.548  28.548 -10.642 1.00 78.19 ? 299 ARG   B CZ   1 
ATOM   4126 N  NH1  . ARG   B 1 268 ? -4.683  29.129 -9.824  1.00 76.32 ? 299 ARG   B NH1  1 
ATOM   4127 N  NH2  . ARG   B 1 268 ? -5.729  29.046 -11.862 1.00 74.61 ? 299 ARG   B NH2  1 
ATOM   4128 N  N    . GLN   B 1 269 ? -8.217  23.026 -6.418  1.00 73.85 ? 300 GLN   B N    1 
ATOM   4129 C  CA   . GLN   B 1 269 ? -8.150  21.654 -6.911  1.00 73.54 ? 300 GLN   B CA   1 
ATOM   4130 C  C    . GLN   B 1 269 ? -9.451  20.883 -6.713  1.00 72.21 ? 300 GLN   B C    1 
ATOM   4131 O  O    . GLN   B 1 269 ? -9.734  19.960 -7.487  1.00 72.69 ? 300 GLN   B O    1 
ATOM   4132 C  CB   . GLN   B 1 269 ? -6.993  20.916 -6.232  1.00 76.06 ? 300 GLN   B CB   1 
ATOM   4133 C  CG   . GLN   B 1 269 ? -5.633  21.530 -6.523  1.00 76.08 ? 300 GLN   B CG   1 
ATOM   4134 C  CD   . GLN   B 1 269 ? -5.399  21.731 -8.011  1.00 80.69 ? 300 GLN   B CD   1 
ATOM   4135 O  OE1  . GLN   B 1 269 ? -4.990  22.811 -8.448  1.00 81.82 ? 300 GLN   B OE1  1 
ATOM   4136 N  NE2  . GLN   B 1 269 ? -5.659  20.690 -8.799  1.00 80.89 ? 300 GLN   B NE2  1 
ATOM   4137 N  N    . LYS   B 1 270 ? -10.253 21.224 -5.699  1.00 69.99 ? 301 LYS   B N    1 
ATOM   4138 C  CA   . LYS   B 1 270 ? -11.471 20.466 -5.429  1.00 67.55 ? 301 LYS   B CA   1 
ATOM   4139 C  C    . LYS   B 1 270 ? -12.755 21.171 -5.838  1.00 64.79 ? 301 LYS   B C    1 
ATOM   4140 O  O    . LYS   B 1 270 ? -13.712 20.495 -6.220  1.00 64.95 ? 301 LYS   B O    1 
ATOM   4141 C  CB   . LYS   B 1 270 ? -11.569 20.101 -3.940  1.00 68.48 ? 301 LYS   B CB   1 
ATOM   4142 C  CG   . LYS   B 1 270 ? -12.510 18.923 -3.685  1.00 63.91 ? 301 LYS   B CG   1 
ATOM   4143 C  CD   . LYS   B 1 270 ? -12.707 18.669 -2.216  1.00 66.57 ? 301 LYS   B CD   1 
ATOM   4144 C  CE   . LYS   B 1 270 ? -11.720 17.676 -1.650  1.00 68.09 ? 301 LYS   B CE   1 
ATOM   4145 N  NZ   . LYS   B 1 270 ? -11.943 17.509 -0.189  1.00 64.16 ? 301 LYS   B NZ   1 
ATOM   4146 N  N    . ALA   B 1 271 ? -12.806 22.499 -5.769  1.00 66.25 ? 302 ALA   B N    1 
ATOM   4147 C  CA   . ALA   B 1 271 ? -14.025 23.223 -6.097  1.00 60.88 ? 302 ALA   B CA   1 
ATOM   4148 C  C    . ALA   B 1 271 ? -14.298 23.187 -7.600  1.00 62.00 ? 302 ALA   B C    1 
ATOM   4149 O  O    . ALA   B 1 271 ? -13.396 23.002 -8.425  1.00 63.71 ? 302 ALA   B O    1 
ATOM   4150 C  CB   . ALA   B 1 271 ? -13.932 24.675 -5.621  1.00 56.81 ? 302 ALA   B CB   1 
ATOM   4151 N  N    . GLY   B 1 272 ? -15.574 23.362 -7.952  1.00 56.20 ? 303 GLY   B N    1 
ATOM   4152 C  CA   . GLY   B 1 272 ? -15.924 23.589 -9.343  1.00 56.91 ? 303 GLY   B CA   1 
ATOM   4153 C  C    . GLY   B 1 272 ? -15.762 25.031 -9.774  1.00 58.79 ? 303 GLY   B C    1 
ATOM   4154 O  O    . GLY   B 1 272 ? -15.501 25.302 -10.953 1.00 58.68 ? 303 GLY   B O    1 
ATOM   4155 N  N    . TYR   B 1 273 ? -15.919 25.968 -8.838  1.00 57.27 ? 304 TYR   B N    1 
ATOM   4156 C  CA   . TYR   B 1 273 ? -15.779 27.400 -9.068  1.00 54.18 ? 304 TYR   B CA   1 
ATOM   4157 C  C    . TYR   B 1 273 ? -15.108 28.017 -7.853  1.00 51.41 ? 304 TYR   B C    1 
ATOM   4158 O  O    . TYR   B 1 273 ? -15.270 27.533 -6.730  1.00 51.83 ? 304 TYR   B O    1 
ATOM   4159 C  CB   . TYR   B 1 273 ? -17.127 28.088 -9.276  1.00 49.73 ? 304 TYR   B CB   1 
ATOM   4160 C  CG   . TYR   B 1 273 ? -17.860 27.725 -10.526 1.00 53.01 ? 304 TYR   B CG   1 
ATOM   4161 C  CD1  . TYR   B 1 273 ? -17.497 28.286 -11.746 1.00 57.57 ? 304 TYR   B CD1  1 
ATOM   4162 C  CD2  . TYR   B 1 273 ? -18.942 26.854 -10.499 1.00 53.13 ? 304 TYR   B CD2  1 
ATOM   4163 C  CE1  . TYR   B 1 273 ? -18.175 27.972 -12.907 1.00 56.37 ? 304 TYR   B CE1  1 
ATOM   4164 C  CE2  . TYR   B 1 273 ? -19.633 26.531 -11.661 1.00 55.91 ? 304 TYR   B CE2  1 
ATOM   4165 C  CZ   . TYR   B 1 273 ? -19.245 27.095 -12.861 1.00 56.99 ? 304 TYR   B CZ   1 
ATOM   4166 O  OH   . TYR   B 1 273 ? -19.924 26.792 -14.027 1.00 68.14 ? 304 TYR   B OH   1 
ATOM   4167 N  N    . ILE   B 1 274 ? -14.365 29.099 -8.074  1.00 49.76 ? 305 ILE   B N    1 
ATOM   4168 C  CA   . ILE   B 1 274 ? -13.729 29.810 -6.966  1.00 43.69 ? 305 ILE   B CA   1 
ATOM   4169 C  C    . ILE   B 1 274 ? -13.477 31.250 -7.401  1.00 48.57 ? 305 ILE   B C    1 
ATOM   4170 O  O    . ILE   B 1 274 ? -13.175 31.513 -8.566  1.00 45.10 ? 305 ILE   B O    1 
ATOM   4171 C  CB   . ILE   B 1 274 ? -12.428 29.099 -6.523  1.00 49.75 ? 305 ILE   B CB   1 
ATOM   4172 C  CG1  . ILE   B 1 274 ? -11.808 29.819 -5.334  1.00 44.98 ? 305 ILE   B CG1  1 
ATOM   4173 C  CG2  . ILE   B 1 274 ? -11.423 29.015 -7.682  1.00 50.90 ? 305 ILE   B CG2  1 
ATOM   4174 C  CD1  . ILE   B 1 274 ? -10.889 28.952 -4.515  1.00 54.38 ? 305 ILE   B CD1  1 
ATOM   4175 N  N    . THR   B 1 275 ? -13.628 32.195 -6.453  1.00 48.89 ? 306 THR   B N    1 
ATOM   4176 C  CA   . THR   B 1 275 ? -13.252 33.569 -6.776  1.00 47.12 ? 306 THR   B CA   1 
ATOM   4177 C  C    . THR   B 1 275 ? -11.870 33.875 -6.229  1.00 47.40 ? 306 THR   B C    1 
ATOM   4178 O  O    . THR   B 1 275 ? -11.513 33.407 -5.138  1.00 47.36 ? 306 THR   B O    1 
ATOM   4179 C  CB   . THR   B 1 275 ? -14.239 34.592 -6.204  1.00 45.57 ? 306 THR   B CB   1 
ATOM   4180 O  OG1  . THR   B 1 275 ? -14.290 34.477 -4.774  1.00 42.58 ? 306 THR   B OG1  1 
ATOM   4181 C  CG2  . THR   B 1 275 ? -15.620 34.408 -6.803  1.00 41.81 ? 306 THR   B CG2  1 
ATOM   4182 N  N    . PRO   B 1 276 ? -11.086 34.660 -6.962  1.00 47.63 ? 307 PRO   B N    1 
ATOM   4183 C  CA   . PRO   B 1 276 ? -9.762  35.053 -6.482  1.00 47.35 ? 307 PRO   B CA   1 
ATOM   4184 C  C    . PRO   B 1 276 ? -9.827  36.304 -5.616  1.00 45.21 ? 307 PRO   B C    1 
ATOM   4185 O  O    . PRO   B 1 276 ? -10.783 37.076 -5.652  1.00 48.02 ? 307 PRO   B O    1 
ATOM   4186 C  CB   . PRO   B 1 276 ? -9.003  35.330 -7.789  1.00 47.40 ? 307 PRO   B CB   1 
ATOM   4187 C  CG   . PRO   B 1 276 ? -10.062 35.891 -8.684  1.00 48.34 ? 307 PRO   B CG   1 
ATOM   4188 C  CD   . PRO   B 1 276 ? -11.349 35.180 -8.314  1.00 49.87 ? 307 PRO   B CD   1 
ATOM   4189 N  N    . VAL   B 1 277 ? -8.770  36.502 -4.834  1.00 45.25 ? 308 VAL   B N    1 
ATOM   4190 C  CA   . VAL   B 1 277 ? -8.598  37.706 -4.038  1.00 49.53 ? 308 VAL   B CA   1 
ATOM   4191 C  C    . VAL   B 1 277 ? -7.187  38.222 -4.280  1.00 54.05 ? 308 VAL   B C    1 
ATOM   4192 O  O    . VAL   B 1 277 ? -6.216  37.511 -4.007  1.00 55.11 ? 308 VAL   B O    1 
ATOM   4193 C  CB   . VAL   B 1 277 ? -8.816  37.463 -2.533  1.00 48.20 ? 308 VAL   B CB   1 
ATOM   4194 C  CG1  . VAL   B 1 277 ? -8.594  38.754 -1.761  1.00 48.37 ? 308 VAL   B CG1  1 
ATOM   4195 C  CG2  . VAL   B 1 277 ? -10.207 36.898 -2.275  1.00 46.67 ? 308 VAL   B CG2  1 
ATOM   4196 N  N    . PRO   B 1 278 ? -7.005  39.460 -4.781  1.00 55.13 ? 309 PRO   B N    1 
ATOM   4197 C  CA   . PRO   B 1 278 ? -8.013  40.416 -5.261  1.00 51.34 ? 309 PRO   B CA   1 
ATOM   4198 C  C    . PRO   B 1 278 ? -8.667  40.033 -6.582  1.00 52.08 ? 309 PRO   B C    1 
ATOM   4199 O  O    . PRO   B 1 278 ? -8.463  38.923 -7.079  1.00 52.69 ? 309 PRO   B O    1 
ATOM   4200 C  CB   . PRO   B 1 278 ? -7.207  41.714 -5.425  1.00 52.36 ? 309 PRO   B CB   1 
ATOM   4201 C  CG   . PRO   B 1 278 ? -5.796  41.279 -5.538  1.00 56.85 ? 309 PRO   B CG   1 
ATOM   4202 C  CD   . PRO   B 1 278 ? -5.695  40.111 -4.614  1.00 55.57 ? 309 PRO   B CD   1 
ATOM   4203 N  N    . GLY   B 1 279 ? -9.445  40.956 -7.147  1.00 49.78 ? 310 GLY   B N    1 
ATOM   4204 C  CA   . GLY   B 1 279 ? -10.078 40.726 -8.424  1.00 44.68 ? 310 GLY   B CA   1 
ATOM   4205 C  C    . GLY   B 1 279 ? -11.325 39.878 -8.383  1.00 43.84 ? 310 GLY   B C    1 
ATOM   4206 O  O    . GLY   B 1 279 ? -11.852 39.530 -9.444  1.00 48.92 ? 310 GLY   B O    1 
ATOM   4207 N  N    . GLY   B 1 280 ? -11.825 39.536 -7.197  1.00 43.70 ? 311 GLY   B N    1 
ATOM   4208 C  CA   . GLY   B 1 280 ? -13.030 38.741 -7.110  1.00 42.12 ? 311 GLY   B CA   1 
ATOM   4209 C  C    . GLY   B 1 280 ? -14.243 39.542 -6.681  1.00 42.69 ? 311 GLY   B C    1 
ATOM   4210 O  O    . GLY   B 1 280 ? -14.870 40.233 -7.492  1.00 39.62 ? 311 GLY   B O    1 
ATOM   4211 N  N    . VAL   B 1 281 ? -14.579 39.442 -5.392  1.00 36.04 ? 312 VAL   B N    1 
ATOM   4212 C  CA   . VAL   B 1 281 ? -15.760 40.118 -4.860  1.00 39.42 ? 312 VAL   B CA   1 
ATOM   4213 C  C    . VAL   B 1 281 ? -15.565 41.632 -4.865  1.00 35.94 ? 312 VAL   B C    1 
ATOM   4214 O  O    . VAL   B 1 281 ? -16.506 42.388 -5.127  1.00 37.56 ? 312 VAL   B O    1 
ATOM   4215 C  CB   . VAL   B 1 281 ? -16.077 39.573 -3.450  1.00 39.02 ? 312 VAL   B CB   1 
ATOM   4216 C  CG1  . VAL   B 1 281 ? -17.216 40.343 -2.807  1.00 39.82 ? 312 VAL   B CG1  1 
ATOM   4217 C  CG2  . VAL   B 1 281 ? -16.438 38.098 -3.526  1.00 39.82 ? 312 VAL   B CG2  1 
ATOM   4218 N  N    . GLY   B 1 282 ? -14.346 42.097 -4.577  1.00 37.15 ? 313 GLY   B N    1 
ATOM   4219 C  CA   . GLY   B 1 282 ? -14.031 43.507 -4.481  1.00 35.35 ? 313 GLY   B CA   1 
ATOM   4220 C  C    . GLY   B 1 282 ? -14.527 44.367 -5.635  1.00 42.00 ? 313 GLY   B C    1 
ATOM   4221 O  O    . GLY   B 1 282 ? -15.245 45.354 -5.434  1.00 41.66 ? 313 GLY   B O    1 
ATOM   4222 N  N    . PRO   B 1 283 ? -14.138 44.030 -6.869  1.00 40.88 ? 314 PRO   B N    1 
ATOM   4223 C  CA   . PRO   B 1 283 ? -14.630 44.811 -8.012  1.00 38.61 ? 314 PRO   B CA   1 
ATOM   4224 C  C    . PRO   B 1 283 ? -16.135 44.764 -8.159  1.00 39.38 ? 314 PRO   B C    1 
ATOM   4225 O  O    . PRO   B 1 283 ? -16.732 45.700 -8.703  1.00 36.69 ? 314 PRO   B O    1 
ATOM   4226 C  CB   . PRO   B 1 283 ? -13.926 44.159 -9.214  1.00 40.43 ? 314 PRO   B CB   1 
ATOM   4227 C  CG   . PRO   B 1 283 ? -12.710 43.564 -8.657  1.00 41.31 ? 314 PRO   B CG   1 
ATOM   4228 C  CD   . PRO   B 1 283 ? -13.098 43.069 -7.274  1.00 41.22 ? 314 PRO   B CD   1 
ATOM   4229 N  N    . MET   B 1 284 ? -16.766 43.681 -7.710  1.00 39.93 ? 315 MET   B N    1 
ATOM   4230 C  CA   . MET   B 1 284 ? -18.220 43.596 -7.781  1.00 41.80 ? 315 MET   B CA   1 
ATOM   4231 C  C    . MET   B 1 284 ? -18.876 44.562 -6.803  1.00 36.63 ? 315 MET   B C    1 
ATOM   4232 O  O    . MET   B 1 284 ? -19.899 45.179 -7.125  1.00 36.58 ? 315 MET   B O    1 
ATOM   4233 C  CB   . MET   B 1 284 ? -18.654 42.153 -7.535  1.00 38.16 ? 315 MET   B CB   1 
ATOM   4234 C  CG   . MET   B 1 284 ? -18.221 41.255 -8.688  1.00 41.17 ? 315 MET   B CG   1 
ATOM   4235 S  SD   . MET   B 1 284 ? -19.210 41.622 -10.141 1.00 44.05 ? 315 MET   B SD   1 
ATOM   4236 C  CE   . MET   B 1 284 ? -20.805 41.022 -9.570  1.00 44.95 ? 315 MET   B CE   1 
ATOM   4237 N  N    . THR   B 1 285 ? -18.278 44.732 -5.621  1.00 35.62 ? 316 THR   B N    1 
ATOM   4238 C  CA   . THR   B 1 285 ? -18.772 45.725 -4.667  1.00 35.67 ? 316 THR   B CA   1 
ATOM   4239 C  C    . THR   B 1 285 ? -18.877 47.098 -5.318  1.00 36.87 ? 316 THR   B C    1 
ATOM   4240 O  O    . THR   B 1 285 ? -19.922 47.759 -5.256  1.00 36.42 ? 316 THR   B O    1 
ATOM   4241 C  CB   . THR   B 1 285 ? -17.841 45.786 -3.457  1.00 36.72 ? 316 THR   B CB   1 
ATOM   4242 O  OG1  . THR   B 1 285 ? -17.881 44.534 -2.766  1.00 39.51 ? 316 THR   B OG1  1 
ATOM   4243 C  CG2  . THR   B 1 285 ? -18.257 46.909 -2.511  1.00 37.48 ? 316 THR   B CG2  1 
ATOM   4244 N  N    . VAL   B 1 286 ? -17.805 47.517 -5.991  1.00 36.71 ? 317 VAL   B N    1 
ATOM   4245 C  CA   . VAL   B 1 286 ? -17.770 48.831 -6.622  1.00 35.57 ? 317 VAL   B CA   1 
ATOM   4246 C  C    . VAL   B 1 286 ? -18.814 48.929 -7.724  1.00 38.17 ? 317 VAL   B C    1 
ATOM   4247 O  O    . VAL   B 1 286 ? -19.491 49.958 -7.876  1.00 36.88 ? 317 VAL   B O    1 
ATOM   4248 C  CB   . VAL   B 1 286 ? -16.353 49.102 -7.158  1.00 40.50 ? 317 VAL   B CB   1 
ATOM   4249 C  CG1  . VAL   B 1 286 ? -16.325 50.375 -7.952  1.00 38.48 ? 317 VAL   B CG1  1 
ATOM   4250 C  CG2  . VAL   B 1 286 ? -15.368 49.162 -6.015  1.00 35.94 ? 317 VAL   B CG2  1 
ATOM   4251 N  N    . ALA   B 1 287 ? -18.949 47.868 -8.528  1.00 35.13 ? 318 ALA   B N    1 
ATOM   4252 C  CA   . ALA   B 1 287 ? -19.905 47.895 -9.626  1.00 36.39 ? 318 ALA   B CA   1 
ATOM   4253 C  C    . ALA   B 1 287 ? -21.343 47.993 -9.119  1.00 36.00 ? 318 ALA   B C    1 
ATOM   4254 O  O    . ALA   B 1 287 ? -22.149 48.741 -9.683  1.00 36.19 ? 318 ALA   B O    1 
ATOM   4255 C  CB   . ALA   B 1 287 ? -19.727 46.649 -10.504 1.00 36.92 ? 318 ALA   B CB   1 
ATOM   4256 N  N    . MET   B 1 288 ? -21.692 47.241 -8.067  1.00 33.03 ? 319 MET   B N    1 
ATOM   4257 C  CA   . MET   B 1 288 ? -23.076 47.284 -7.574  1.00 36.71 ? 319 MET   B CA   1 
ATOM   4258 C  C    . MET   B 1 288 ? -23.429 48.642 -6.957  1.00 35.93 ? 319 MET   B C    1 
ATOM   4259 O  O    . MET   B 1 288 ? -24.592 49.066 -7.008  1.00 34.85 ? 319 MET   B O    1 
ATOM   4260 C  CB   . MET   B 1 288 ? -23.327 46.155 -6.562  1.00 33.17 ? 319 MET   B CB   1 
ATOM   4261 C  CG   . MET   B 1 288 ? -22.931 44.749 -7.036  1.00 34.36 ? 319 MET   B CG   1 
ATOM   4262 S  SD   . MET   B 1 288 ? -23.486 44.241 -8.698  1.00 40.40 ? 319 MET   B SD   1 
ATOM   4263 C  CE   . MET   B 1 288 ? -25.222 44.677 -8.688  1.00 39.16 ? 319 MET   B CE   1 
ATOM   4264 N  N    . LEU   B 1 289 ? -22.451 49.344 -6.382  1.00 35.31 ? 320 LEU   B N    1 
ATOM   4265 C  CA   . LEU   B 1 289 ? -22.676 50.724 -5.953  1.00 31.20 ? 320 LEU   B CA   1 
ATOM   4266 C  C    . LEU   B 1 289 ? -23.087 51.610 -7.127  1.00 35.05 ? 320 LEU   B C    1 
ATOM   4267 O  O    . LEU   B 1 289 ? -23.908 52.522 -6.968  1.00 33.19 ? 320 LEU   B O    1 
ATOM   4268 C  CB   . LEU   B 1 289 ? -21.410 51.274 -5.299  1.00 34.00 ? 320 LEU   B CB   1 
ATOM   4269 C  CG   . LEU   B 1 289 ? -21.403 52.769 -4.956  1.00 41.16 ? 320 LEU   B CG   1 
ATOM   4270 C  CD1  . LEU   B 1 289 ? -22.537 53.115 -4.011  1.00 30.97 ? 320 LEU   B CD1  1 
ATOM   4271 C  CD2  . LEU   B 1 289 ? -20.074 53.195 -4.365  1.00 34.94 ? 320 LEU   B CD2  1 
ATOM   4272 N  N    . MET   B 1 290 ? -22.494 51.380 -8.311  1.00 34.05 ? 321 MET   B N    1 
ATOM   4273 C  CA   . MET   B 1 290 ? -22.898 52.129 -9.500  1.00 35.40 ? 321 MET   B CA   1 
ATOM   4274 C  C    . MET   B 1 290 ? -24.356 51.848 -9.848  1.00 34.83 ? 321 MET   B C    1 
ATOM   4275 O  O    . MET   B 1 290 ? -25.117 52.773 -10.157 1.00 36.21 ? 321 MET   B O    1 
ATOM   4276 C  CB   . MET   B 1 290 ? -21.983 51.785 -10.689 1.00 34.32 ? 321 MET   B CB   1 
ATOM   4277 C  CG   . MET   B 1 290 ? -20.497 52.008 -10.421 1.00 33.87 ? 321 MET   B CG   1 
ATOM   4278 S  SD   . MET   B 1 290 ? -20.176 53.705 -9.892  1.00 41.01 ? 321 MET   B SD   1 
ATOM   4279 C  CE   . MET   B 1 290 ? -19.654 53.504 -8.186  1.00 35.97 ? 321 MET   B CE   1 
ATOM   4280 N  N    . LYS   B 1 291 ? -24.766 50.574 -9.785  1.00 34.10 ? 322 LYS   B N    1 
ATOM   4281 C  CA   . LYS   B 1 291 ? -26.178 50.226 -9.961  1.00 35.55 ? 322 LYS   B CA   1 
ATOM   4282 C  C    . LYS   B 1 291 ? -27.065 50.998 -8.984  1.00 38.20 ? 322 LYS   B C    1 
ATOM   4283 O  O    . LYS   B 1 291 ? -28.089 51.573 -9.377  1.00 35.78 ? 322 LYS   B O    1 
ATOM   4284 C  CB   . LYS   B 1 291 ? -26.374 48.716 -9.782  1.00 39.18 ? 322 LYS   B CB   1 
ATOM   4285 C  CG   . LYS   B 1 291 ? -25.881 47.848 -10.939 1.00 36.40 ? 322 LYS   B CG   1 
ATOM   4286 C  CD   . LYS   B 1 291 ? -26.993 47.561 -11.952 1.00 41.74 ? 322 LYS   B CD   1 
ATOM   4287 C  CE   . LYS   B 1 291 ? -26.447 46.795 -13.171 1.00 44.28 ? 322 LYS   B CE   1 
ATOM   4288 N  NZ   . LYS   B 1 291 ? -27.472 46.633 -14.237 1.00 41.58 ? 322 LYS   B NZ   1 
ATOM   4289 N  N    . ASN   B 1 292 ? -26.680 51.031 -7.699  1.00 35.94 ? 323 ASN   B N    1 
ATOM   4290 C  CA   . ASN   B 1 292 ? -27.508 51.702 -6.695  1.00 35.87 ? 323 ASN   B CA   1 
ATOM   4291 C  C    . ASN   B 1 292 ? -27.564 53.207 -6.910  1.00 33.92 ? 323 ASN   B C    1 
ATOM   4292 O  O    . ASN   B 1 292 ? -28.573 53.841 -6.583  1.00 35.56 ? 323 ASN   B O    1 
ATOM   4293 C  CB   . ASN   B 1 292 ? -26.987 51.419 -5.283  1.00 34.69 ? 323 ASN   B CB   1 
ATOM   4294 C  CG   . ASN   B 1 292 ? -27.396 50.065 -4.764  1.00 40.49 ? 323 ASN   B CG   1 
ATOM   4295 O  OD1  . ASN   B 1 292 ? -28.221 49.384 -5.360  1.00 39.22 ? 323 ASN   B OD1  1 
ATOM   4296 N  ND2  . ASN   B 1 292 ? -26.850 49.683 -3.608  1.00 41.83 ? 323 ASN   B ND2  1 
ATOM   4297 N  N    . THR   B 1 293 ? -26.487 53.801 -7.419  1.00 32.63 ? 324 THR   B N    1 
ATOM   4298 C  CA   . THR   B 1 293 ? -26.469 55.249 -7.596  1.00 33.29 ? 324 THR   B CA   1 
ATOM   4299 C  C    . THR   B 1 293 ? -27.424 55.693 -8.700  1.00 36.73 ? 324 THR   B C    1 
ATOM   4300 O  O    . THR   B 1 293 ? -28.117 56.708 -8.552  1.00 33.69 ? 324 THR   B O    1 
ATOM   4301 C  CB   . THR   B 1 293 ? -25.048 55.730 -7.878  1.00 35.03 ? 324 THR   B CB   1 
ATOM   4302 O  OG1  . THR   B 1 293 ? -24.200 55.379 -6.777  1.00 34.76 ? 324 THR   B OG1  1 
ATOM   4303 C  CG2  . THR   B 1 293 ? -25.025 57.239 -8.065  1.00 34.62 ? 324 THR   B CG2  1 
ATOM   4304 N  N    . ILE   B 1 294 ? -27.482 54.952 -9.817  1.00 35.79 ? 325 ILE   B N    1 
ATOM   4305 C  CA   . ILE   B 1 294 ? -28.463 55.295 -10.846 1.00 37.90 ? 325 ILE   B CA   1 
ATOM   4306 C  C    . ILE   B 1 294 ? -29.878 55.011 -10.344 1.00 39.12 ? 325 ILE   B C    1 
ATOM   4307 O  O    . ILE   B 1 294 ? -30.804 55.788 -10.606 1.00 38.86 ? 325 ILE   B O    1 
ATOM   4308 C  CB   . ILE   B 1 294 ? -28.150 54.580 -12.180 1.00 41.25 ? 325 ILE   B CB   1 
ATOM   4309 C  CG1  . ILE   B 1 294 ? -29.149 55.002 -13.262 1.00 38.00 ? 325 ILE   B CG1  1 
ATOM   4310 C  CG2  . ILE   B 1 294 ? -28.156 53.077 -12.030 1.00 38.94 ? 325 ILE   B CG2  1 
ATOM   4311 C  CD1  . ILE   B 1 294 ? -29.160 56.494 -13.537 1.00 39.61 ? 325 ILE   B CD1  1 
ATOM   4312 N  N    . ILE   B 1 295 ? -30.063 53.928 -9.575  1.00 38.16 ? 326 ILE   B N    1 
ATOM   4313 C  CA   . ILE   B 1 295 ? -31.363 53.668 -8.952  1.00 40.80 ? 326 ILE   B CA   1 
ATOM   4314 C  C    . ILE   B 1 295 ? -31.800 54.863 -8.098  1.00 42.22 ? 326 ILE   B C    1 
ATOM   4315 O  O    . ILE   B 1 295 ? -32.945 55.325 -8.183  1.00 40.75 ? 326 ILE   B O    1 
ATOM   4316 C  CB   . ILE   B 1 295 ? -31.306 52.372 -8.123  1.00 39.87 ? 326 ILE   B CB   1 
ATOM   4317 C  CG1  . ILE   B 1 295 ? -31.346 51.142 -9.018  1.00 37.86 ? 326 ILE   B CG1  1 
ATOM   4318 C  CG2  . ILE   B 1 295 ? -32.442 52.312 -7.161  1.00 40.98 ? 326 ILE   B CG2  1 
ATOM   4319 C  CD1  . ILE   B 1 295 ? -31.143 49.846 -8.247  1.00 36.06 ? 326 ILE   B CD1  1 
ATOM   4320 N  N    . ALA   B 1 296 ? -30.885 55.397 -7.279  1.00 40.11 ? 327 ALA   B N    1 
ATOM   4321 C  CA   . ALA   B 1 296 ? -31.222 56.543 -6.434  1.00 41.71 ? 327 ALA   B CA   1 
ATOM   4322 C  C    . ALA   B 1 296 ? -31.533 57.788 -7.259  1.00 43.27 ? 327 ALA   B C    1 
ATOM   4323 O  O    . ALA   B 1 296 ? -32.461 58.541 -6.934  1.00 40.15 ? 327 ALA   B O    1 
ATOM   4324 C  CB   . ALA   B 1 296 ? -30.087 56.828 -5.458  1.00 39.64 ? 327 ALA   B CB   1 
ATOM   4325 N  N    . ALA   B 1 297 ? -30.768 58.031 -8.324  1.00 41.21 ? 328 ALA   B N    1 
ATOM   4326 C  CA   . ALA   B 1 297 ? -31.026 59.208 -9.143  1.00 40.05 ? 328 ALA   B CA   1 
ATOM   4327 C  C    . ALA   B 1 297 ? -32.406 59.132 -9.790  1.00 44.76 ? 328 ALA   B C    1 
ATOM   4328 O  O    . ALA   B 1 297 ? -33.099 60.148 -9.912  1.00 46.87 ? 328 ALA   B O    1 
ATOM   4329 C  CB   . ALA   B 1 297 ? -29.929 59.362 -10.203 1.00 41.44 ? 328 ALA   B CB   1 
ATOM   4330 N  N    . LYS   B 1 298 ? -32.824 57.933 -10.202 1.00 44.55 ? 329 LYS   B N    1 
ATOM   4331 C  CA   . LYS   B 1 298 ? -34.137 57.760 -10.815 1.00 45.31 ? 329 LYS   B CA   1 
ATOM   4332 C  C    . LYS   B 1 298 ? -35.275 57.881 -9.810  1.00 49.60 ? 329 LYS   B C    1 
ATOM   4333 O  O    . LYS   B 1 298 ? -36.423 58.061 -10.225 1.00 50.48 ? 329 LYS   B O    1 
ATOM   4334 C  CB   . LYS   B 1 298 ? -34.211 56.408 -11.518 1.00 42.17 ? 329 LYS   B CB   1 
ATOM   4335 C  CG   . LYS   B 1 298 ? -33.253 56.306 -12.688 1.00 43.59 ? 329 LYS   B CG   1 
ATOM   4336 C  CD   . LYS   B 1 298 ? -33.404 54.995 -13.420 1.00 43.68 ? 329 LYS   B CD   1 
ATOM   4337 C  CE   . LYS   B 1 298 ? -33.127 55.177 -14.897 1.00 44.77 ? 329 LYS   B CE   1 
ATOM   4338 N  NZ   . LYS   B 1 298 ? -32.932 53.873 -15.580 1.00 42.16 ? 329 LYS   B NZ   1 
ATOM   4339 N  N    . LYS   B 1 299 ? -34.982 57.784 -8.508  1.00 48.99 ? 330 LYS   B N    1 
ATOM   4340 C  CA   . LYS   B 1 299 ? -35.990 57.917 -7.454  1.00 50.80 ? 330 LYS   B CA   1 
ATOM   4341 C  C    . LYS   B 1 299 ? -37.142 56.929 -7.643  1.00 55.76 ? 330 LYS   B C    1 
ATOM   4342 O  O    . LYS   B 1 299 ? -38.308 57.269 -7.437  1.00 62.54 ? 330 LYS   B O    1 
ATOM   4343 C  CB   . LYS   B 1 299 ? -36.517 59.352 -7.379  1.00 51.54 ? 330 LYS   B CB   1 
ATOM   4344 C  CG   . LYS   B 1 299 ? -35.459 60.399 -7.064  1.00 55.63 ? 330 LYS   B CG   1 
ATOM   4345 C  CD   . LYS   B 1 299 ? -36.058 61.804 -7.072  1.00 59.10 ? 330 LYS   B CD   1 
ATOM   4346 C  CE   . LYS   B 1 299 ? -35.211 62.747 -7.914  1.00 64.38 ? 330 LYS   B CE   1 
ATOM   4347 N  NZ   . LYS   B 1 299 ? -36.006 63.863 -8.510  1.00 71.77 ? 330 LYS   B NZ   1 
ATOM   4348 N  N    . VAL   B 1 300 ? -36.819 55.694 -8.044  1.00 51.16 ? 331 VAL   B N    1 
ATOM   4349 C  CA   . VAL   B 1 300 ? -37.848 54.670 -8.235  1.00 55.55 ? 331 VAL   B CA   1 
ATOM   4350 C  C    . VAL   B 1 300 ? -38.317 54.021 -6.936  1.00 62.63 ? 331 VAL   B C    1 
ATOM   4351 O  O    . VAL   B 1 300 ? -39.356 53.343 -6.935  1.00 61.34 ? 331 VAL   B O    1 
ATOM   4352 C  CB   . VAL   B 1 300 ? -37.359 53.582 -9.214  1.00 55.06 ? 331 VAL   B CB   1 
ATOM   4353 C  CG1  . VAL   B 1 300 ? -37.436 54.084 -10.647 1.00 54.07 ? 331 VAL   B CG1  1 
ATOM   4354 C  CG2  . VAL   B 1 300 ? -35.939 53.175 -8.898  1.00 53.36 ? 331 VAL   B CG2  1 
ATOM   4355 N  N    . LEU   B 1 301 ? -37.606 54.211 -5.828  1.00 56.65 ? 332 LEU   B N    1 
ATOM   4356 C  CA   . LEU   B 1 301 ? -37.983 53.568 -4.565  1.00 61.68 ? 332 LEU   B CA   1 
ATOM   4357 C  C    . LEU   B 1 301 ? -39.002 54.392 -3.780  1.00 62.12 ? 332 LEU   B C    1 
ATOM   4358 O  O    . LEU   B 1 301 ? -38.991 55.621 -3.824  1.00 66.52 ? 332 LEU   B O    1 
ATOM   4359 C  CB   . LEU   B 1 301 ? -36.748 53.318 -3.699  1.00 61.25 ? 332 LEU   B CB   1 
ATOM   4360 C  CG   . LEU   B 1 301 ? -35.803 52.175 -4.091  1.00 56.96 ? 332 LEU   B CG   1 
ATOM   4361 C  CD1  . LEU   B 1 301 ? -36.498 50.829 -4.021  1.00 58.35 ? 332 LEU   B CD1  1 
ATOM   4362 C  CD2  . LEU   B 1 301 ? -35.262 52.382 -5.464  1.00 65.19 ? 332 LEU   B CD2  1 
HETATM 4363 C  C10  . A1L24 C 2 .   ? -50.851 32.423 17.746  1.00 36.10 ? 401 A1L24 A C10  1 
HETATM 4364 C  C13  . A1L24 C 2 .   ? -51.271 32.985 18.944  1.00 35.09 ? 401 A1L24 A C13  1 
HETATM 4365 C  C15  . A1L24 C 2 .   ? -52.038 30.819 19.624  1.00 39.58 ? 401 A1L24 A C15  1 
HETATM 4366 C  C17  . A1L24 C 2 .   ? -50.989 31.073 17.502  1.00 37.95 ? 401 A1L24 A C17  1 
HETATM 4367 C  C21  . A1L24 C 2 .   ? -52.927 27.634 21.607  1.00 44.21 ? 401 A1L24 A C21  1 
HETATM 4368 C  C22  . A1L24 C 2 .   ? -51.999 26.428 21.621  1.00 41.71 ? 401 A1L24 A C22  1 
HETATM 4369 C  C26  . A1L24 C 2 .   ? -54.490 26.333 20.118  1.00 52.23 ? 401 A1L24 A C26  1 
HETATM 4370 C  C02  . A1L24 C 2 .   ? -50.462 39.154 14.631  1.00 29.32 ? 401 A1L24 A C02  1 
HETATM 4371 C  C04  . A1L24 C 2 .   ? -50.763 36.960 14.103  1.00 32.08 ? 401 A1L24 A C04  1 
HETATM 4372 C  C05  . A1L24 C 2 .   ? -49.954 36.610 15.169  1.00 27.33 ? 401 A1L24 A C05  1 
HETATM 4373 C  C06  . A1L24 C 2 .   ? -49.403 37.595 15.967  1.00 30.61 ? 401 A1L24 A C06  1 
HETATM 4374 C  C08  . A1L24 C 2 .   ? -50.503 34.598 16.476  1.00 34.77 ? 401 A1L24 A C08  1 
HETATM 4375 C  C14  . A1L24 C 2 .   ? -51.875 32.168 19.891  1.00 35.18 ? 401 A1L24 A C14  1 
HETATM 4376 C  C16  . A1L24 C 2 .   ? -51.595 30.252 18.427  1.00 37.10 ? 401 A1L24 A C16  1 
HETATM 4377 C  C18  . A1L24 C 2 .   ? -52.681 29.929 20.670  1.00 39.76 ? 401 A1L24 A C18  1 
HETATM 4378 C  C23  . A1L24 C 2 .   ? -54.383 27.270 21.314  1.00 49.65 ? 401 A1L24 A C23  1 
HETATM 4379 C  C27  . A1L24 C 2 .   ? -55.890 26.340 19.508  1.00 61.66 ? 401 A1L24 A C27  1 
HETATM 4380 N  N01  . A1L24 C 2 .   ? -49.688 38.853 15.671  1.00 30.33 ? 401 A1L24 A N01  1 
HETATM 4381 N  N03  . A1L24 C 2 .   ? -51.007 38.236 13.851  1.00 30.03 ? 401 A1L24 A N03  1 
HETATM 4382 N  N07  . A1L24 C 2 .   ? -49.662 35.230 15.476  1.00 28.60 ? 401 A1L24 A N07  1 
HETATM 4383 N  N09  . A1L24 C 2 .   ? -50.185 33.229 16.759  1.00 35.89 ? 401 A1L24 A N09  1 
HETATM 4384 N  N11  . A1L24 C 2 .   ? -51.323 35.899 13.294  1.00 28.75 ? 401 A1L24 A N11  1 
HETATM 4385 N  N20  . A1L24 C 2 .   ? -52.378 28.517 20.590  1.00 38.70 ? 401 A1L24 A N20  1 
HETATM 4386 N  N28  . A1L24 C 2 .   ? -56.394 27.279 18.661  1.00 67.03 ? 401 A1L24 A N28  1 
HETATM 4387 N  N29  . A1L24 C 2 .   ? -57.658 26.926 18.339  1.00 64.58 ? 401 A1L24 A N29  1 
HETATM 4388 N  N30  . A1L24 C 2 .   ? -57.931 25.804 18.963  1.00 69.24 ? 401 A1L24 A N30  1 
HETATM 4389 N  N31  . A1L24 C 2 .   ? -56.867 25.410 19.694  1.00 65.14 ? 401 A1L24 A N31  1 
HETATM 4390 N  N34  . A1L24 C 2 .   ? -50.754 40.549 14.355  1.00 27.52 ? 401 A1L24 A N34  1 
HETATM 4391 O  O12  . A1L24 C 2 .   ? -51.410 35.176 17.010  1.00 33.23 ? 401 A1L24 A O12  1 
HETATM 4392 O  O19  . A1L24 C 2 .   ? -53.367 30.379 21.538  1.00 39.21 ? 401 A1L24 A O19  1 
HETATM 4393 O  O24  . A1L24 C 2 .   ? -52.117 25.541 22.498  1.00 44.69 ? 401 A1L24 A O24  1 
HETATM 4394 O  O25  . A1L24 C 2 .   ? -51.075 26.350 20.763  1.00 42.16 ? 401 A1L24 A O25  1 
HETATM 4395 O  O33  . A1L24 C 2 .   ? -48.685 37.295 16.879  1.00 31.07 ? 401 A1L24 A O33  1 
HETATM 4396 CL CL32 . A1L24 C 2 .   ? -50.421 30.419 15.947  1.00 45.08 ? 401 A1L24 A CL32 1 
HETATM 4397 P  PA   . NAD   D 3 .   ? -46.278 30.624 6.425   0.71 45.76 ? 402 NAD   A PA   1 
HETATM 4398 O  O1A  . NAD   D 3 .   ? -47.213 29.764 5.631   0.71 52.06 ? 402 NAD   A O1A  1 
HETATM 4399 O  O2A  . NAD   D 3 .   ? -46.132 32.081 6.140   0.71 45.09 ? 402 NAD   A O2A  1 
HETATM 4400 O  O5B  . NAD   D 3 .   ? -44.777 29.984 6.356   0.71 41.50 ? 402 NAD   A O5B  1 
HETATM 4401 C  C5B  . NAD   D 3 .   ? -44.558 28.617 6.150   0.71 40.56 ? 402 NAD   A C5B  1 
HETATM 4402 C  C4B  . NAD   D 3 .   ? -43.055 28.461 6.055   0.71 40.54 ? 402 NAD   A C4B  1 
HETATM 4403 O  O4B  . NAD   D 3 .   ? -42.723 27.065 6.023   0.71 42.89 ? 402 NAD   A O4B  1 
HETATM 4404 C  C3B  . NAD   D 3 .   ? -42.460 29.066 4.783   0.71 39.01 ? 402 NAD   A C3B  1 
HETATM 4405 O  O3B  . NAD   D 3 .   ? -41.275 29.739 5.138   0.71 34.20 ? 402 NAD   A O3B  1 
HETATM 4406 C  C2B  . NAD   D 3 .   ? -42.137 27.825 3.940   0.71 39.31 ? 402 NAD   A C2B  1 
HETATM 4407 O  O2B  . NAD   D 3 .   ? -41.129 28.076 3.003   0.71 36.36 ? 402 NAD   A O2B  1 
HETATM 4408 C  C1B  . NAD   D 3 .   ? -41.766 26.824 5.035   0.71 40.54 ? 402 NAD   A C1B  1 
HETATM 4409 N  N9A  . NAD   D 3 .   ? -41.855 25.454 4.566   0.71 40.26 ? 402 NAD   A N9A  1 
HETATM 4410 C  C8A  . NAD   D 3 .   ? -42.851 24.907 3.806   0.71 39.35 ? 402 NAD   A C8A  1 
HETATM 4411 N  N7A  . NAD   D 3 .   ? -42.634 23.657 3.524   0.71 38.86 ? 402 NAD   A N7A  1 
HETATM 4412 C  C5A  . NAD   D 3 .   ? -41.438 23.332 4.106   0.71 35.90 ? 402 NAD   A C5A  1 
HETATM 4413 C  C6A  . NAD   D 3 .   ? -40.640 22.170 4.187   0.71 39.60 ? 402 NAD   A C6A  1 
HETATM 4414 N  N6A  . NAD   D 3 .   ? -40.970 21.013 3.630   0.71 42.34 ? 402 NAD   A N6A  1 
HETATM 4415 N  N1A  . NAD   D 3 .   ? -39.479 22.231 4.868   0.71 38.28 ? 402 NAD   A N1A  1 
HETATM 4416 C  C2A  . NAD   D 3 .   ? -39.143 23.390 5.438   0.71 37.64 ? 402 NAD   A C2A  1 
HETATM 4417 N  N3A  . NAD   D 3 .   ? -39.816 24.526 5.427   0.71 40.25 ? 402 NAD   A N3A  1 
HETATM 4418 C  C4A  . NAD   D 3 .   ? -40.948 24.457 4.753   0.71 37.94 ? 402 NAD   A C4A  1 
HETATM 4419 O  O3   . NAD   D 3 .   ? -46.649 30.317 8.009   0.71 49.75 ? 402 NAD   A O3   1 
HETATM 4420 P  PN   . NAD   D 3 .   ? -45.946 30.890 9.381   0.71 52.45 ? 402 NAD   A PN   1 
HETATM 4421 O  O1N  . NAD   D 3 .   ? -46.648 32.158 9.796   0.71 48.11 ? 402 NAD   A O1N  1 
HETATM 4422 O  O2N  . NAD   D 3 .   ? -44.449 30.842 9.397   0.71 44.67 ? 402 NAD   A O2N  1 
HETATM 4423 O  O5D  . NAD   D 3 .   ? -46.468 29.689 10.371  0.71 50.34 ? 402 NAD   A O5D  1 
HETATM 4424 C  C5D  . NAD   D 3 .   ? -46.218 28.341 10.031  0.71 48.07 ? 402 NAD   A C5D  1 
HETATM 4425 C  C4D  . NAD   D 3 .   ? -46.830 27.471 11.097  0.71 46.71 ? 402 NAD   A C4D  1 
HETATM 4426 O  O4D  . NAD   D 3 .   ? -46.542 28.091 12.361  0.71 49.40 ? 402 NAD   A O4D  1 
HETATM 4427 C  C3D  . NAD   D 3 .   ? -48.369 27.333 11.065  0.71 49.84 ? 402 NAD   A C3D  1 
HETATM 4428 O  O3D  . NAD   D 3 .   ? -48.692 26.050 11.562  0.71 44.87 ? 402 NAD   A O3D  1 
HETATM 4429 C  C2D  . NAD   D 3 .   ? -48.833 28.441 12.035  0.71 51.56 ? 402 NAD   A C2D  1 
HETATM 4430 O  O2D  . NAD   D 3 .   ? -50.104 28.303 12.608  0.71 51.46 ? 402 NAD   A O2D  1 
HETATM 4431 C  C1D  . NAD   D 3 .   ? -47.721 28.256 13.074  0.71 46.39 ? 402 NAD   A C1D  1 
HETATM 4432 N  N1N  . NAD   D 3 .   ? -47.591 29.359 14.055  0.71 48.00 ? 402 NAD   A N1N  1 
HETATM 4433 C  C2N  . NAD   D 3 .   ? -47.630 29.046 15.332  0.71 44.10 ? 402 NAD   A C2N  1 
HETATM 4434 C  C3N  . NAD   D 3 .   ? -47.488 29.991 16.314  0.71 42.84 ? 402 NAD   A C3N  1 
HETATM 4435 C  C7N  . NAD   D 3 .   ? -47.554 29.556 17.752  0.71 40.85 ? 402 NAD   A C7N  1 
HETATM 4436 O  O7N  . NAD   D 3 .   ? -47.620 28.342 17.976  0.71 39.20 ? 402 NAD   A O7N  1 
HETATM 4437 N  N7N  . NAD   D 3 .   ? -47.533 30.539 18.647  0.71 30.74 ? 402 NAD   A N7N  1 
HETATM 4438 C  C4N  . NAD   D 3 .   ? -47.332 31.336 15.938  0.71 42.12 ? 402 NAD   A C4N  1 
HETATM 4439 C  C5N  . NAD   D 3 .   ? -47.294 31.639 14.590  0.71 41.04 ? 402 NAD   A C5N  1 
HETATM 4440 C  C6N  . NAD   D 3 .   ? -47.419 30.637 13.652  0.71 43.29 ? 402 NAD   A C6N  1 
HETATM 4441 P  P    . PO4   E 4 .   ? -42.291 31.534 2.005   1.00 39.49 ? 403 PO4   A P    1 
HETATM 4442 O  O1   . PO4   E 4 .   ? -41.747 32.690 1.091   1.00 41.95 ? 403 PO4   A O1   1 
HETATM 4443 O  O2   . PO4   E 4 .   ? -43.829 31.404 1.790   1.00 38.56 ? 403 PO4   A O2   1 
HETATM 4444 O  O3   . PO4   E 4 .   ? -41.580 30.188 1.678   1.00 35.36 ? 403 PO4   A O3   1 
HETATM 4445 O  O4   . PO4   E 4 .   ? -42.005 31.948 3.504   1.00 42.07 ? 403 PO4   A O4   1 
HETATM 4446 P  P    . PO4   F 4 .   ? -19.917 39.588 15.329  1.00 42.50 ? 404 PO4   A P    1 
HETATM 4447 O  O1   . PO4   F 4 .   ? -18.665 40.485 15.590  1.00 46.65 ? 404 PO4   A O1   1 
HETATM 4448 O  O2   . PO4   F 4 .   ? -20.405 39.697 13.842  1.00 40.84 ? 404 PO4   A O2   1 
HETATM 4449 O  O3   . PO4   F 4 .   ? -19.579 38.080 15.615  1.00 41.02 ? 404 PO4   A O3   1 
HETATM 4450 O  O4   . PO4   F 4 .   ? -21.059 40.052 16.318  1.00 42.37 ? 404 PO4   A O4   1 
HETATM 4451 C  C10  . A1L24 G 2 .   ? -14.756 47.184 -0.485  1.00 42.22 ? 401 A1L24 B C10  1 
HETATM 4452 C  C13  . A1L24 G 2 .   ? -14.956 47.917 -1.636  1.00 38.90 ? 401 A1L24 B C13  1 
HETATM 4453 C  C15  . A1L24 G 2 .   ? -12.979 46.937 -2.543  1.00 42.37 ? 401 A1L24 B C15  1 
HETATM 4454 C  C17  . A1L24 G 2 .   ? -13.685 46.323 -0.376  1.00 43.79 ? 401 A1L24 B C17  1 
HETATM 4455 C  C21  . A1L24 G 2 .   ? -10.381 45.183 -4.827  1.00 49.83 ? 401 A1L24 B C21  1 
HETATM 4456 C  C22  . A1L24 G 2 .   ? -10.336 43.663 -4.851  1.00 47.66 ? 401 A1L24 B C22  1 
HETATM 4457 C  C26  . A1L24 G 2 .   ? -8.367  45.096 -3.293  1.00 57.45 ? 401 A1L24 B C26  1 
HETATM 4458 C  C02  . A1L24 G 2 .   ? -19.341 51.715 3.323   1.00 32.89 ? 401 A1L24 B C02  1 
HETATM 4459 C  C04  . A1L24 G 2 .   ? -17.534 50.333 3.522   1.00 33.45 ? 401 A1L24 B C04  1 
HETATM 4460 C  C05  . A1L24 G 2 .   ? -18.008 49.575 2.480   1.00 36.60 ? 401 A1L24 B C05  1 
HETATM 4461 C  C06  . A1L24 G 2 .   ? -19.197 49.934 1.874   1.00 35.34 ? 401 A1L24 B C06  1 
HETATM 4462 C  C08  . A1L24 G 2 .   ? -16.363 48.506 0.964   1.00 40.64 ? 401 A1L24 B C08  1 
HETATM 4463 C  C14  . A1L24 G 2 .   ? -14.057 47.792 -2.673  1.00 40.15 ? 401 A1L24 B C14  1 
HETATM 4464 C  C16  . A1L24 G 2 .   ? -12.781 46.184 -1.409  1.00 41.21 ? 401 A1L24 B C16  1 
HETATM 4465 C  C18  . A1L24 G 2 .   ? -11.998 46.780 -3.694  1.00 45.53 ? 401 A1L24 B C18  1 
HETATM 4466 C  C23  . A1L24 G 2 .   ? -9.006  45.765 -4.507  1.00 52.46 ? 401 A1L24 B C23  1 
HETATM 4467 C  C27  . A1L24 G 2 .   ? -7.041  45.783 -2.978  1.00 67.25 ? 401 A1L24 B C27  1 
HETATM 4468 N  N01  . A1L24 G 2 .   ? -19.832 51.006 2.338   1.00 31.91 ? 401 A1L24 B N01  1 
HETATM 4469 N  N03  . A1L24 G 2 .   ? -18.210 51.391 3.928   1.00 34.71 ? 401 A1L24 B N03  1 
HETATM 4470 N  N07  . A1L24 G 2 .   ? -17.284 48.403 2.049   1.00 32.89 ? 401 A1L24 B N07  1 
HETATM 4471 N  N09  . A1L24 G 2 .   ? -15.696 47.278 0.606   1.00 41.79 ? 401 A1L24 B N09  1 
HETATM 4472 N  N11  . A1L24 G 2 .   ? -16.294 49.929 4.137   1.00 38.30 ? 401 A1L24 B N11  1 
HETATM 4473 N  N20  . A1L24 G 2 .   ? -11.317 45.500 -3.775  1.00 41.35 ? 401 A1L24 B N20  1 
HETATM 4474 N  N28  . A1L24 G 2 .   ? -5.928  45.754 -3.761  1.00 69.88 ? 401 A1L24 B N28  1 
HETATM 4475 N  N29  . A1L24 G 2 .   ? -4.982  46.487 -3.139  1.00 77.26 ? 401 A1L24 B N29  1 
HETATM 4476 N  N30  . A1L24 G 2 .   ? -5.482  46.962 -2.018  1.00 77.79 ? 401 A1L24 B N30  1 
HETATM 4477 N  N31  . A1L24 G 2 .   ? -6.757  46.546 -1.881  1.00 71.51 ? 401 A1L24 B N31  1 
HETATM 4478 N  N34  . A1L24 G 2 .   ? -20.079 52.876 3.779   1.00 33.18 ? 401 A1L24 B N34  1 
HETATM 4479 O  O12  . A1L24 G 2 .   ? -16.184 49.550 0.422   1.00 38.57 ? 401 A1L24 B O12  1 
HETATM 4480 O  O19  . A1L24 G 2 .   ? -11.841 47.657 -4.479  1.00 45.54 ? 401 A1L24 B O19  1 
HETATM 4481 O  O24  . A1L24 G 2 .   ? -9.893  43.085 -5.859  1.00 46.35 ? 401 A1L24 B O24  1 
HETATM 4482 O  O25  . A1L24 G 2 .   ? -10.760 42.992 -3.870  1.00 46.01 ? 401 A1L24 B O25  1 
HETATM 4483 O  O33  . A1L24 G 2 .   ? -19.617 49.295 0.958   1.00 37.91 ? 401 A1L24 B O33  1 
HETATM 4484 CL CL32 . A1L24 G 2 .   ? -13.479 45.396 1.119   1.00 50.04 ? 401 A1L24 B CL32 1 
HETATM 4485 P  PA   . NAD   H 3 .   ? -16.531 41.821 10.957  0.74 48.75 ? 402 NAD   B PA   1 
HETATM 4486 O  O1A  . NAD   H 3 .   ? -15.282 41.677 11.760  0.74 54.00 ? 402 NAD   B O1A  1 
HETATM 4487 O  O2A  . NAD   H 3 .   ? -17.587 42.822 11.276  0.74 50.00 ? 402 NAD   B O2A  1 
HETATM 4488 O  O5B  . NAD   H 3 .   ? -17.258 40.368 10.806  0.74 46.99 ? 402 NAD   B O5B  1 
HETATM 4489 C  C5B  . NAD   H 3 .   ? -16.506 39.220 10.510  0.74 44.75 ? 402 NAD   B C5B  1 
HETATM 4490 C  C4B  . NAD   H 3 .   ? -17.425 38.057 10.792  0.74 42.77 ? 402 NAD   B C4B  1 
HETATM 4491 O  O4B  . NAD   H 3 .   ? -16.673 36.834 10.802  0.74 45.03 ? 402 NAD   B O4B  1 
HETATM 4492 C  C3B  . NAD   H 3 .   ? -18.107 38.161 12.155  0.74 42.03 ? 402 NAD   B C3B  1 
HETATM 4493 O  O3B  . NAD   H 3 .   ? -19.484 38.044 11.898  0.74 37.85 ? 402 NAD   B O3B  1 
HETATM 4494 C  C2B  . NAD   H 3 .   ? -17.553 36.946 12.924  0.74 43.86 ? 402 NAD   B C2B  1 
HETATM 4495 O  O2B  . NAD   H 3 .   ? -18.440 36.435 13.885  0.74 40.17 ? 402 NAD   B O2B  1 
HETATM 4496 C  C1B  . NAD   H 3 .   ? -17.193 35.986 11.788  0.74 42.74 ? 402 NAD   B C1B  1 
HETATM 4497 N  N9A  . NAD   H 3 .   ? -16.220 34.995 12.212  0.74 45.04 ? 402 NAD   B N9A  1 
HETATM 4498 C  C8A  . NAD   H 3 .   ? -15.152 35.173 13.046  0.74 45.15 ? 402 NAD   B C8A  1 
HETATM 4499 N  N7A  . NAD   H 3 .   ? -14.479 34.079 13.250  0.74 46.32 ? 402 NAD   B N7A  1 
HETATM 4500 C  C5A  . NAD   H 3 .   ? -15.123 33.103 12.533  0.74 44.48 ? 402 NAD   B C5A  1 
HETATM 4501 C  C6A  . NAD   H 3 .   ? -14.927 31.718 12.324  0.74 43.45 ? 402 NAD   B C6A  1 
HETATM 4502 N  N6A  . NAD   H 3 .   ? -13.934 31.030 12.868  0.74 44.61 ? 402 NAD   B N6A  1 
HETATM 4503 N  N1A  . NAD   H 3 .   ? -15.791 31.060 11.534  0.74 41.81 ? 402 NAD   B N1A  1 
HETATM 4504 C  C2A  . NAD   H 3 .   ? -16.791 31.750 10.984  0.74 43.19 ? 402 NAD   B C2A  1 
HETATM 4505 N  N3A  . NAD   H 3 .   ? -17.062 33.037 11.104  0.74 43.62 ? 402 NAD   B N3A  1 
HETATM 4506 C  C4A  . NAD   H 3 .   ? -16.209 33.672 11.888  0.74 42.26 ? 402 NAD   B C4A  1 
HETATM 4507 O  O3   . NAD   H 3 .   ? -16.010 41.981 9.400   0.74 52.54 ? 402 NAD   B O3   1 
HETATM 4508 P  PN   . NAD   H 3 .   ? -16.831 42.475 8.066   0.74 59.09 ? 402 NAD   B PN   1 
HETATM 4509 O  O1N  . NAD   H 3 .   ? -16.902 43.984 8.047   0.74 54.62 ? 402 NAD   B O1N  1 
HETATM 4510 O  O2N  . NAD   H 3 .   ? -18.046 41.677 7.709   0.74 50.94 ? 402 NAD   B O2N  1 
HETATM 4511 O  O5D  . NAD   H 3 .   ? -15.650 42.051 7.005   0.74 57.36 ? 402 NAD   B O5D  1 
HETATM 4512 C  C5D  . NAD   H 3 .   ? -15.161 40.725 6.982   0.74 54.14 ? 402 NAD   B C5D  1 
HETATM 4513 C  C4D  . NAD   H 3 .   ? -14.247 40.533 5.794   0.74 53.61 ? 402 NAD   B C4D  1 
HETATM 4514 O  O4D  . NAD   H 3 .   ? -14.969 40.857 4.594   0.74 52.80 ? 402 NAD   B O4D  1 
HETATM 4515 C  C3D  . NAD   H 3 .   ? -12.992 41.433 5.748   0.74 57.18 ? 402 NAD   B C3D  1 
HETATM 4516 O  O3D  . NAD   H 3 .   ? -11.973 40.684 5.118   0.74 56.60 ? 402 NAD   B O3D  1 
HETATM 4517 C  C2D  . NAD   H 3 .   ? -13.469 42.596 4.860   0.74 54.22 ? 402 NAD   B C2D  1 
HETATM 4518 O  O2D  . NAD   H 3 .   ? -12.500 43.392 4.241   0.74 56.14 ? 402 NAD   B O2D  1 
HETATM 4519 C  C1D  . NAD   H 3 .   ? -14.187 41.719 3.836   0.74 54.40 ? 402 NAD   B C1D  1 
HETATM 4520 N  N1N  . NAD   H 3 .   ? -14.975 42.502 2.859   0.74 51.01 ? 402 NAD   B N1N  1 
HETATM 4521 C  C2N  . NAD   H 3 .   ? -14.738 42.346 1.564   0.74 47.60 ? 402 NAD   B C2N  1 
HETATM 4522 C  C3N  . NAD   H 3 .   ? -15.463 43.036 0.624   0.74 47.51 ? 402 NAD   B C3N  1 
HETATM 4523 C  C7N  . NAD   H 3 .   ? -15.223 42.875 -0.862  0.74 45.36 ? 402 NAD   B C7N  1 
HETATM 4524 O  O7N  . NAD   H 3 .   ? -14.552 41.926 -1.285  0.74 43.20 ? 402 NAD   B O7N  1 
HETATM 4525 N  N7N  . NAD   H 3 .   ? -15.800 43.807 -1.609  0.74 35.36 ? 402 NAD   B N7N  1 
HETATM 4526 C  C4N  . NAD   H 3 .   ? -16.434 43.936 1.082   0.74 46.54 ? 402 NAD   B C4N  1 
HETATM 4527 C  C5N  . NAD   H 3 .   ? -16.659 44.088 2.435   0.74 49.09 ? 402 NAD   B C5N  1 
HETATM 4528 C  C6N  . NAD   H 3 .   ? -15.912 43.354 3.329   0.74 49.65 ? 402 NAD   B C6N  1 
HETATM 4529 O  O    . HOH   I 5 .   ? -42.859 41.517 33.481  1.00 47.86 ? 501 HOH   A O    1 
HETATM 4530 O  O    . HOH   I 5 .   ? -22.059 24.918 15.528  1.00 47.30 ? 502 HOH   A O    1 
HETATM 4531 O  O    . HOH   I 5 .   ? -59.194 41.332 27.991  1.00 43.11 ? 503 HOH   A O    1 
HETATM 4532 O  O    . HOH   I 5 .   ? -41.579 30.438 -4.929  1.00 46.97 ? 504 HOH   A O    1 
HETATM 4533 O  O    . HOH   I 5 .   ? -41.025 34.570 38.139  1.00 45.72 ? 505 HOH   A O    1 
HETATM 4534 O  O    . HOH   I 5 .   ? -47.048 16.456 13.350  1.00 50.57 ? 506 HOH   A O    1 
HETATM 4535 O  O    . HOH   I 5 .   ? -67.892 38.545 8.748   1.00 47.18 ? 507 HOH   A O    1 
HETATM 4536 O  O    . HOH   I 5 .   ? -47.190 39.790 6.531   1.00 47.45 ? 508 HOH   A O    1 
HETATM 4537 O  O    . HOH   I 5 .   ? -57.515 39.717 11.291  1.00 34.45 ? 509 HOH   A O    1 
HETATM 4538 O  O    . HOH   I 5 .   ? -21.706 36.071 23.160  1.00 45.28 ? 510 HOH   A O    1 
HETATM 4539 O  O    . HOH   I 5 .   ? -48.924 37.778 40.133  1.00 43.91 ? 511 HOH   A O    1 
HETATM 4540 O  O    . HOH   I 5 .   ? -42.440 41.003 10.595  1.00 41.66 ? 512 HOH   A O    1 
HETATM 4541 O  O    . HOH   I 5 .   ? -62.438 52.923 9.298   1.00 49.72 ? 513 HOH   A O    1 
HETATM 4542 O  O    . HOH   I 5 .   ? -48.966 54.259 28.953  1.00 53.36 ? 514 HOH   A O    1 
HETATM 4543 O  O    . HOH   I 5 .   ? -43.910 33.305 4.609   1.00 39.24 ? 515 HOH   A O    1 
HETATM 4544 O  O    . HOH   I 5 .   ? -30.010 29.247 26.755  1.00 48.00 ? 516 HOH   A O    1 
HETATM 4545 O  O    . HOH   I 5 .   ? -29.723 20.708 22.697  1.00 44.62 ? 517 HOH   A O    1 
HETATM 4546 O  O    . HOH   I 5 .   ? -58.568 38.571 7.578   1.00 35.50 ? 518 HOH   A O    1 
HETATM 4547 O  O    . HOH   I 5 .   ? -31.031 51.909 13.885  1.00 53.44 ? 519 HOH   A O    1 
HETATM 4548 O  O    . HOH   I 5 .   ? -45.030 23.564 20.817  1.00 35.99 ? 520 HOH   A O    1 
HETATM 4549 O  O    . HOH   I 5 .   ? -54.364 34.189 12.777  1.00 33.83 ? 521 HOH   A O    1 
HETATM 4550 O  O    . HOH   I 5 .   ? -47.407 56.645 19.651  1.00 53.64 ? 522 HOH   A O    1 
HETATM 4551 O  O    . HOH   I 5 .   ? -53.005 40.513 2.683   1.00 43.46 ? 523 HOH   A O    1 
HETATM 4552 O  O    . HOH   I 5 .   ? -48.714 25.183 20.984  1.00 36.35 ? 524 HOH   A O    1 
HETATM 4553 O  O    . HOH   I 5 .   ? -61.132 38.518 21.776  1.00 41.45 ? 525 HOH   A O    1 
HETATM 4554 O  O    . HOH   I 5 .   ? -40.116 43.029 23.122  1.00 36.19 ? 526 HOH   A O    1 
HETATM 4555 O  O    . HOH   I 5 .   ? -49.928 44.535 13.966  1.00 35.59 ? 527 HOH   A O    1 
HETATM 4556 O  O    . HOH   I 5 .   ? -51.494 36.840 3.936   1.00 51.90 ? 528 HOH   A O    1 
HETATM 4557 O  O    . HOH   I 5 .   ? -39.527 11.810 7.780   1.00 55.65 ? 529 HOH   A O    1 
HETATM 4558 O  O    . HOH   I 5 .   ? -60.082 36.490 10.296  1.00 46.85 ? 530 HOH   A O    1 
HETATM 4559 O  O    . HOH   I 5 .   ? -43.729 53.731 42.826  1.00 43.79 ? 531 HOH   A O    1 
HETATM 4560 O  O    . HOH   I 5 .   ? -18.945 41.198 19.866  1.00 50.92 ? 532 HOH   A O    1 
HETATM 4561 O  O    . HOH   I 5 .   ? -49.834 24.141 36.315  1.00 46.68 ? 533 HOH   A O    1 
HETATM 4562 O  O    . HOH   I 5 .   ? -58.861 58.096 11.352  1.00 51.19 ? 534 HOH   A O    1 
HETATM 4563 O  O    . HOH   I 5 .   ? -31.664 16.882 15.849  1.00 47.98 ? 535 HOH   A O    1 
HETATM 4564 O  O    . HOH   I 5 .   ? -59.026 43.031 30.026  1.00 36.62 ? 536 HOH   A O    1 
HETATM 4565 O  O    . HOH   I 5 .   ? -25.202 34.036 23.374  1.00 40.95 ? 537 HOH   A O    1 
HETATM 4566 O  O    . HOH   I 5 .   ? -35.810 35.041 30.522  1.00 56.60 ? 538 HOH   A O    1 
HETATM 4567 O  O    . HOH   I 5 .   ? -33.846 43.289 18.665  1.00 37.24 ? 539 HOH   A O    1 
HETATM 4568 O  O    . HOH   I 5 .   ? -19.552 42.596 17.037  1.00 54.66 ? 540 HOH   A O    1 
HETATM 4569 O  O    . HOH   I 5 .   ? -45.333 35.961 14.478  1.00 42.13 ? 541 HOH   A O    1 
HETATM 4570 O  O    . HOH   I 5 .   ? -22.998 40.516 13.923  1.00 34.31 ? 542 HOH   A O    1 
HETATM 4571 O  O    . HOH   I 5 .   ? -57.301 36.875 10.432  1.00 36.21 ? 543 HOH   A O    1 
HETATM 4572 O  O    . HOH   I 5 .   ? -52.837 30.155 24.207  1.00 38.07 ? 544 HOH   A O    1 
HETATM 4573 O  O    . HOH   I 5 .   ? -24.838 39.316 15.617  1.00 34.34 ? 545 HOH   A O    1 
HETATM 4574 O  O    . HOH   I 5 .   ? -47.289 17.430 17.007  1.00 52.79 ? 546 HOH   A O    1 
HETATM 4575 O  O    . HOH   I 5 .   ? -26.148 29.453 25.272  1.00 41.53 ? 547 HOH   A O    1 
HETATM 4576 O  O    . HOH   I 5 .   ? -19.774 37.925 22.325  1.00 47.34 ? 548 HOH   A O    1 
HETATM 4577 O  O    . HOH   I 5 .   ? -40.391 34.171 3.563   1.00 29.81 ? 549 HOH   A O    1 
HETATM 4578 O  O    . HOH   I 5 .   ? -35.618 30.875 9.421   1.00 36.62 ? 550 HOH   A O    1 
HETATM 4579 O  O    . HOH   I 5 .   ? -49.596 36.867 7.069   1.00 43.20 ? 551 HOH   A O    1 
HETATM 4580 O  O    . HOH   I 5 .   ? -41.771 30.219 9.216   1.00 37.76 ? 552 HOH   A O    1 
HETATM 4581 O  O    . HOH   I 5 .   ? -50.930 55.522 10.563  1.00 42.83 ? 553 HOH   A O    1 
HETATM 4582 O  O    . HOH   I 5 .   ? -44.891 18.533 19.104  1.00 44.99 ? 554 HOH   A O    1 
HETATM 4583 O  O    . HOH   I 5 .   ? -59.664 50.645 28.502  1.00 51.17 ? 555 HOH   A O    1 
HETATM 4584 O  O    . HOH   I 5 .   ? -23.025 20.573 18.558  1.00 56.75 ? 556 HOH   A O    1 
HETATM 4585 O  O    . HOH   I 5 .   ? -47.739 46.497 13.460  1.00 33.43 ? 557 HOH   A O    1 
HETATM 4586 O  O    . HOH   I 5 .   ? -29.984 51.396 19.779  1.00 51.22 ? 558 HOH   A O    1 
HETATM 4587 O  O    . HOH   I 5 .   ? -59.141 35.743 31.352  1.00 42.71 ? 559 HOH   A O    1 
HETATM 4588 O  O    . HOH   I 5 .   ? -45.902 37.278 16.880  1.00 32.89 ? 560 HOH   A O    1 
HETATM 4589 O  O    . HOH   I 5 .   ? -37.814 20.237 3.856   1.00 46.03 ? 561 HOH   A O    1 
HETATM 4590 O  O    . HOH   I 5 .   ? -55.275 32.788 27.032  1.00 36.16 ? 562 HOH   A O    1 
HETATM 4591 O  O    . HOH   I 5 .   ? -27.938 22.646 23.134  1.00 48.11 ? 563 HOH   A O    1 
HETATM 4592 O  O    . HOH   I 5 .   ? -58.667 37.449 0.631   1.00 36.38 ? 564 HOH   A O    1 
HETATM 4593 O  O    . HOH   I 5 .   ? -59.434 30.068 22.193  1.00 54.26 ? 565 HOH   A O    1 
HETATM 4594 O  O    . HOH   I 5 .   ? -45.727 39.649 17.240  1.00 29.99 ? 566 HOH   A O    1 
HETATM 4595 O  O    . HOH   I 5 .   ? -21.253 22.366 18.842  1.00 56.21 ? 567 HOH   A O    1 
HETATM 4596 O  O    . HOH   I 5 .   ? -38.839 30.717 38.030  1.00 53.46 ? 568 HOH   A O    1 
HETATM 4597 O  O    . HOH   I 5 .   ? -33.123 36.401 27.392  1.00 51.61 ? 569 HOH   A O    1 
HETATM 4598 O  O    . HOH   I 5 .   ? -26.391 38.848 11.966  1.00 32.57 ? 570 HOH   A O    1 
HETATM 4599 O  O    . HOH   I 5 .   ? -59.535 39.670 -0.802  1.00 46.49 ? 571 HOH   A O    1 
HETATM 4600 O  O    . HOH   I 5 .   ? -53.270 55.084 9.190   1.00 45.62 ? 572 HOH   A O    1 
HETATM 4601 O  O    . HOH   I 5 .   ? -25.326 42.449 25.705  1.00 48.24 ? 573 HOH   A O    1 
HETATM 4602 O  O    . HOH   I 5 .   ? -47.526 53.009 23.844  1.00 43.23 ? 574 HOH   A O    1 
HETATM 4603 O  O    . HOH   I 5 .   ? -62.601 35.709 6.426   1.00 44.65 ? 575 HOH   A O    1 
HETATM 4604 O  O    . HOH   I 5 .   ? -58.321 47.631 -0.261  1.00 38.28 ? 576 HOH   A O    1 
HETATM 4605 O  O    . HOH   I 5 .   ? -57.946 34.173 6.719   1.00 51.06 ? 577 HOH   A O    1 
HETATM 4606 O  O    . HOH   I 5 .   ? -43.415 35.590 5.274   1.00 35.64 ? 578 HOH   A O    1 
HETATM 4607 O  O    . HOH   I 5 .   ? -54.934 33.561 29.721  1.00 36.27 ? 579 HOH   A O    1 
HETATM 4608 O  O    . HOH   I 5 .   ? -43.889 48.302 36.977  1.00 47.88 ? 580 HOH   A O    1 
HETATM 4609 O  O    . HOH   I 5 .   ? -47.315 25.180 18.334  1.00 37.67 ? 581 HOH   A O    1 
HETATM 4610 O  O    . HOH   I 5 .   ? -51.122 33.426 35.038  1.00 39.57 ? 582 HOH   A O    1 
HETATM 4611 O  O    . HOH   I 5 .   ? -50.285 43.447 11.615  1.00 41.92 ? 583 HOH   A O    1 
HETATM 4612 O  O    . HOH   I 5 .   ? -50.020 57.115 32.698  1.00 51.21 ? 584 HOH   A O    1 
HETATM 4613 O  O    . HOH   I 5 .   ? -66.104 38.638 6.722   1.00 44.03 ? 585 HOH   A O    1 
HETATM 4614 O  O    . HOH   I 5 .   ? -50.930 32.157 27.483  1.00 37.22 ? 586 HOH   A O    1 
HETATM 4615 O  O    . HOH   I 5 .   ? -44.884 36.212 7.893   1.00 42.58 ? 587 HOH   A O    1 
HETATM 4616 O  O    . HOH   I 5 .   ? -59.587 27.258 15.964  1.00 56.16 ? 588 HOH   A O    1 
HETATM 4617 O  O    . HOH   I 5 .   ? -27.886 18.204 22.022  1.00 58.89 ? 589 HOH   A O    1 
HETATM 4618 O  O    . HOH   I 5 .   ? -50.466 41.398 2.011   1.00 38.74 ? 590 HOH   A O    1 
HETATM 4619 O  O    . HOH   I 5 .   ? -51.475 29.888 29.150  1.00 42.59 ? 591 HOH   A O    1 
HETATM 4620 O  O    . HOH   I 5 .   ? -45.749 54.918 11.359  1.00 50.39 ? 592 HOH   A O    1 
HETATM 4621 O  O    . HOH   I 5 .   ? -57.044 30.822 27.168  1.00 50.32 ? 593 HOH   A O    1 
HETATM 4622 O  O    . HOH   I 5 .   ? -46.620 40.520 43.965  1.00 49.20 ? 594 HOH   A O    1 
HETATM 4623 O  O    . HOH   I 5 .   ? -25.776 31.807 25.073  1.00 49.78 ? 595 HOH   A O    1 
HETATM 4624 O  O    . HOH   I 5 .   ? -25.454 46.133 18.345  1.00 47.13 ? 596 HOH   A O    1 
HETATM 4625 O  O    . HOH   I 5 .   ? -65.129 36.636 6.007   1.00 51.50 ? 597 HOH   A O    1 
HETATM 4626 O  O    . HOH   I 5 .   ? -41.972 53.963 8.157   1.00 50.48 ? 598 HOH   A O    1 
HETATM 4627 O  O    . HOH   I 5 .   ? -53.349 32.043 11.887  1.00 44.97 ? 599 HOH   A O    1 
HETATM 4628 O  O    . HOH   I 5 .   ? -53.042 31.648 26.207  1.00 39.06 ? 600 HOH   A O    1 
HETATM 4629 O  O    . HOH   I 5 .   ? -61.471 36.917 30.270  1.00 42.14 ? 601 HOH   A O    1 
HETATM 4630 O  O    . HOH   I 5 .   ? -23.144 45.421 14.013  1.00 51.56 ? 602 HOH   A O    1 
HETATM 4631 O  O    . HOH   I 5 .   ? -53.194 28.410 28.031  1.00 46.36 ? 603 HOH   A O    1 
HETATM 4632 O  O    . HOH   J 5 .   ? -31.313 47.152 1.518   1.00 42.39 ? 501 HOH   B O    1 
HETATM 4633 O  O    . HOH   J 5 .   ? -42.107 47.058 5.367   1.00 45.24 ? 502 HOH   B O    1 
HETATM 4634 O  O    . HOH   J 5 .   ? -3.646  29.254 -2.153  1.00 61.74 ? 503 HOH   B O    1 
HETATM 4635 O  O    . HOH   J 5 .   ? -15.553 60.437 -9.938  1.00 45.84 ? 504 HOH   B O    1 
HETATM 4636 O  O    . HOH   J 5 .   ? -16.820 69.583 5.987   1.00 53.70 ? 505 HOH   B O    1 
HETATM 4637 O  O    . HOH   J 5 .   ? -14.389 39.980 13.242  1.00 53.90 ? 506 HOH   B O    1 
HETATM 4638 O  O    . HOH   J 5 .   ? -30.762 62.031 -12.486 1.00 50.51 ? 507 HOH   B O    1 
HETATM 4639 O  O    . HOH   J 5 .   ? -5.679  63.260 8.925   1.00 49.13 ? 508 HOH   B O    1 
HETATM 4640 O  O    . HOH   J 5 .   ? -34.946 31.734 -6.032  1.00 40.75 ? 509 HOH   B O    1 
HETATM 4641 O  O    . HOH   J 5 .   ? -10.022 52.873 10.092  1.00 49.88 ? 510 HOH   B O    1 
HETATM 4642 O  O    . HOH   J 5 .   ? -30.241 47.899 -5.025  1.00 39.19 ? 511 HOH   B O    1 
HETATM 4643 O  O    . HOH   J 5 .   ? -27.459 45.365 6.382   1.00 50.65 ? 512 HOH   B O    1 
HETATM 4644 O  O    . HOH   J 5 .   ? -6.987  23.360 1.014   1.00 60.83 ? 513 HOH   B O    1 
HETATM 4645 O  O    . HOH   J 5 .   ? -28.105 39.021 -12.536 1.00 55.30 ? 514 HOH   B O    1 
HETATM 4646 O  O    . HOH   J 5 .   ? -13.029 50.915 4.350   1.00 32.99 ? 515 HOH   B O    1 
HETATM 4647 O  O    . HOH   J 5 .   ? -27.892 49.145 -15.492 1.00 49.52 ? 516 HOH   B O    1 
HETATM 4648 O  O    . HOH   J 5 .   ? -38.836 30.500 -6.191  1.00 45.12 ? 517 HOH   B O    1 
HETATM 4649 O  O    . HOH   J 5 .   ? -23.429 55.181 4.256   1.00 36.64 ? 518 HOH   B O    1 
HETATM 4650 O  O    . HOH   J 5 .   ? -6.740  32.427 2.679   1.00 57.54 ? 519 HOH   B O    1 
HETATM 4651 O  O    . HOH   J 5 .   ? -12.419 56.539 9.842   1.00 44.11 ? 520 HOH   B O    1 
HETATM 4652 O  O    . HOH   J 5 .   ? -30.355 38.552 -9.905  1.00 52.54 ? 521 HOH   B O    1 
HETATM 4653 O  O    . HOH   J 5 .   ? -31.908 54.754 -18.136 1.00 44.82 ? 522 HOH   B O    1 
HETATM 4654 O  O    . HOH   J 5 .   ? -7.428  52.193 -5.638  1.00 50.14 ? 523 HOH   B O    1 
HETATM 4655 O  O    . HOH   J 5 .   ? -29.763 46.567 3.996   1.00 40.51 ? 524 HOH   B O    1 
HETATM 4656 O  O    . HOH   J 5 .   ? -12.173 59.431 -4.318  1.00 46.19 ? 525 HOH   B O    1 
HETATM 4657 O  O    . HOH   J 5 .   ? -12.408 54.686 6.886   1.00 38.40 ? 526 HOH   B O    1 
HETATM 4658 O  O    . HOH   J 5 .   ? -38.377 34.676 1.853   1.00 33.29 ? 527 HOH   B O    1 
HETATM 4659 O  O    . HOH   J 5 .   ? -7.489  59.095 -0.913  1.00 49.45 ? 528 HOH   B O    1 
HETATM 4660 O  O    . HOH   J 5 .   ? -30.748 65.379 7.384   1.00 48.19 ? 529 HOH   B O    1 
HETATM 4661 O  O    . HOH   J 5 .   ? -24.994 66.142 -11.628 1.00 49.44 ? 530 HOH   B O    1 
HETATM 4662 O  O    . HOH   J 5 .   ? -17.306 61.394 -11.830 1.00 45.10 ? 531 HOH   B O    1 
HETATM 4663 O  O    . HOH   J 5 .   ? -31.728 62.727 -10.051 1.00 53.47 ? 532 HOH   B O    1 
HETATM 4664 O  O    . HOH   J 5 .   ? -7.539  57.355 10.455  1.00 49.49 ? 533 HOH   B O    1 
HETATM 4665 O  O    . HOH   J 5 .   ? -26.302 55.027 5.294   1.00 40.31 ? 534 HOH   B O    1 
HETATM 4666 O  O    . HOH   J 5 .   ? -12.705 51.214 -9.894  1.00 39.24 ? 535 HOH   B O    1 
HETATM 4667 O  O    . HOH   J 5 .   ? -34.561 43.851 -0.420  1.00 41.36 ? 536 HOH   B O    1 
HETATM 4668 O  O    . HOH   J 5 .   ? -26.439 47.776 7.859   1.00 49.38 ? 537 HOH   B O    1 
HETATM 4669 O  O    . HOH   J 5 .   ? -29.855 66.017 -19.317 1.00 50.38 ? 538 HOH   B O    1 
HETATM 4670 O  O    . HOH   J 5 .   ? -25.528 55.232 1.836   1.00 34.09 ? 539 HOH   B O    1 
HETATM 4671 O  O    . HOH   J 5 .   ? -7.156  64.290 13.244  1.00 50.14 ? 540 HOH   B O    1 
HETATM 4672 O  O    . HOH   J 5 .   ? -17.610 49.190 10.441  1.00 50.08 ? 541 HOH   B O    1 
HETATM 4673 O  O    . HOH   J 5 .   ? -7.370  61.823 10.107  1.00 45.42 ? 542 HOH   B O    1 
HETATM 4674 O  O    . HOH   J 5 .   ? -17.737 27.997 20.308  1.00 50.28 ? 543 HOH   B O    1 
HETATM 4675 O  O    . HOH   J 5 .   ? -15.172 47.616 -10.416 1.00 42.66 ? 544 HOH   B O    1 
HETATM 4676 O  O    . HOH   J 5 .   ? -44.133 32.691 -2.330  1.00 52.24 ? 545 HOH   B O    1 
HETATM 4677 O  O    . HOH   J 5 .   ? -32.199 33.316 -9.037  1.00 47.10 ? 546 HOH   B O    1 
HETATM 4678 O  O    . HOH   J 5 .   ? -12.232 47.344 -7.193  1.00 47.46 ? 547 HOH   B O    1 
HETATM 4679 O  O    . HOH   J 5 .   ? -14.195 56.828 6.453   1.00 38.50 ? 548 HOH   B O    1 
HETATM 4680 O  O    . HOH   J 5 .   ? -21.104 45.923 3.085   1.00 44.76 ? 549 HOH   B O    1 
HETATM 4681 O  O    . HOH   J 5 .   ? -36.727 35.081 5.464   1.00 32.59 ? 550 HOH   B O    1 
HETATM 4682 O  O    . HOH   J 5 .   ? -21.361 47.128 0.758   1.00 40.09 ? 551 HOH   B O    1 
HETATM 4683 O  O    . HOH   J 5 .   ? -32.754 39.982 -6.013  1.00 40.29 ? 552 HOH   B O    1 
HETATM 4684 O  O    . HOH   J 5 .   ? -27.551 64.814 10.485  1.00 50.51 ? 553 HOH   B O    1 
HETATM 4685 O  O    . HOH   J 5 .   ? -15.977 28.286 12.250  1.00 50.33 ? 554 HOH   B O    1 
HETATM 4686 O  O    . HOH   J 5 .   ? -25.241 25.014 -6.999  1.00 51.69 ? 555 HOH   B O    1 
HETATM 4687 O  O    . HOH   J 5 .   ? -22.613 24.694 -6.824  1.00 47.45 ? 556 HOH   B O    1 
HETATM 4688 O  O    . HOH   J 5 .   ? -20.147 51.171 -1.204  1.00 34.88 ? 557 HOH   B O    1 
HETATM 4689 O  O    . HOH   J 5 .   ? -29.576 63.580 9.274   1.00 50.27 ? 558 HOH   B O    1 
HETATM 4690 O  O    . HOH   J 5 .   ? -44.524 33.837 0.227   1.00 51.17 ? 559 HOH   B O    1 
HETATM 4691 O  O    . HOH   J 5 .   ? -17.988 63.381 18.882  1.00 46.97 ? 560 HOH   B O    1 
HETATM 4692 O  O    . HOH   J 5 .   ? -19.618 38.794 7.905   1.00 38.45 ? 561 HOH   B O    1 
HETATM 4693 O  O    . HOH   J 5 .   ? -27.905 20.028 -2.823  1.00 54.34 ? 562 HOH   B O    1 
HETATM 4694 O  O    . HOH   J 5 .   ? -11.596 57.728 18.220  1.00 55.73 ? 563 HOH   B O    1 
HETATM 4695 O  O    . HOH   J 5 .   ? -10.557 29.463 -14.921 1.00 53.22 ? 564 HOH   B O    1 
HETATM 4696 O  O    . HOH   J 5 .   ? -34.588 45.764 -4.685  1.00 48.30 ? 565 HOH   B O    1 
HETATM 4697 O  O    . HOH   J 5 .   ? -24.479 23.190 3.803   1.00 49.19 ? 566 HOH   B O    1 
HETATM 4698 O  O    . HOH   J 5 .   ? -16.094 70.219 10.284  1.00 52.52 ? 567 HOH   B O    1 
HETATM 4699 O  O    . HOH   J 5 .   ? -19.848 52.699 16.237  1.00 53.62 ? 568 HOH   B O    1 
HETATM 4700 O  O    . HOH   J 5 .   ? -23.223 48.948 0.754   1.00 37.10 ? 569 HOH   B O    1 
HETATM 4701 O  O    . HOH   J 5 .   ? -21.804 43.848 12.222  1.00 43.45 ? 570 HOH   B O    1 
HETATM 4702 O  O    . HOH   J 5 .   ? -15.947 49.750 13.141  1.00 51.25 ? 571 HOH   B O    1 
HETATM 4703 O  O    . HOH   J 5 .   ? -31.456 29.075 -8.658  1.00 44.81 ? 572 HOH   B O    1 
HETATM 4704 O  O    . HOH   J 5 .   ? -4.383  54.253 0.011   1.00 54.32 ? 573 HOH   B O    1 
HETATM 4705 O  O    . HOH   J 5 .   ? -17.660 64.490 -11.177 1.00 49.95 ? 574 HOH   B O    1 
HETATM 4706 O  O    . HOH   J 5 .   ? -28.555 49.048 -19.372 1.00 50.80 ? 575 HOH   B O    1 
HETATM 4707 O  O    . HOH   J 5 .   ? -16.917 48.861 -17.774 1.00 46.85 ? 576 HOH   B O    1 
HETATM 4708 O  O    . HOH   J 5 .   ? -12.449 39.486 -1.718  1.00 45.73 ? 577 HOH   B O    1 
HETATM 4709 O  O    . HOH   J 5 .   ? -21.263 45.253 9.788   1.00 42.61 ? 578 HOH   B O    1 
HETATM 4710 O  O    . HOH   J 5 .   ? -29.335 50.001 -11.808 1.00 42.64 ? 579 HOH   B O    1 
HETATM 4711 O  O    . HOH   J 5 .   ? -9.704  58.740 -1.963  1.00 52.91 ? 580 HOH   B O    1 
HETATM 4712 O  O    . HOH   J 5 .   ? -9.343  36.038 -12.566 1.00 54.09 ? 581 HOH   B O    1 
HETATM 4713 O  O    . HOH   J 5 .   ? -13.267 48.518 -9.075  1.00 45.51 ? 582 HOH   B O    1 
HETATM 4714 O  O    . HOH   J 5 .   ? -43.684 37.712 3.715   1.00 44.40 ? 583 HOH   B O    1 
HETATM 4715 O  O    . HOH   J 5 .   ? -12.174 48.050 4.889   1.00 48.67 ? 584 HOH   B O    1 
HETATM 4716 O  O    . HOH   J 5 .   ? -34.827 47.831 -7.670  1.00 64.27 ? 585 HOH   B O    1 
# 
